3thc: Difference between revisions

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<StructureSection load='3thc' size='340' side='right'caption='[[3thc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3thc' size='340' side='right'caption='[[3thc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3thc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3thc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lhd|3lhd]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLB1, ELNR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3thc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thc OCA], [https://pdbe.org/3thc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thc RCSB], [https://www.ebi.ac.uk/pdbsum/3thc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thc ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3thc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thc OCA], [https://pdbe.org/3thc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thc RCSB], [https://www.ebi.ac.uk/pdbsum/3thc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thc ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref>  GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref>  GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref>  Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>
[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:[https://omim.org/entry/230500 230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:1487238</ref> <ref>PMID:8213816</ref> <ref>PMID:11511921</ref> <ref>PMID:12393180</ref> <ref>PMID:10338095</ref> <ref>PMID:10839995</ref> <ref>PMID:10737981</ref> <ref>PMID:15365997</ref> <ref>PMID:15714521</ref> <ref>PMID:15791924</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref>  GM1-gangliosidosis 2 (GM1G2) [MIM:[https://omim.org/entry/230600 230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:8213816</ref> <ref>PMID:10737981</ref> <ref>PMID:15714521</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:12644936</ref>  GM1-gangliosidosis 3 (GM1G3) [MIM:[https://omim.org/entry/230650 230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1909089</ref> <ref>PMID:1907800</ref> <ref>PMID:11511921</ref> <ref>PMID:16941474</ref> <ref>PMID:17309651</ref> <ref>PMID:19472408</ref> <ref>PMID:8198123</ref> <ref>PMID:7586649</ref> <ref>PMID:11511921</ref> <ref>PMID:15986423</ref>  Mucopolysaccharidosis 4B (MPS4B) [MIM:[https://omim.org/entry/253010 253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:1928092</ref> <ref>PMID:16941474</ref> <ref>PMID:16538002</ref> <ref>PMID:19472408</ref> <ref>PMID:11511921</ref> <ref>PMID:7586649</ref> <ref>PMID:12393180</ref>  
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN]] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref>  Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>
[https://www.uniprot.org/uniprot/BGAL_HUMAN BGAL_HUMAN] Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.<ref>PMID:8922281</ref>  Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.<ref>PMID:8922281</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-galactosidase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ohto, U]]
[[Category: Ohto U]]
[[Category: Shimizu, T]]
[[Category: Shimizu T]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosylation]]
[[Category: Hydrolase]]
[[Category: Tim-barrel domain]]

Latest revision as of 20:32, 1 November 2023

Crystal structure of human beta-galactosidase in complex with galactoseCrystal structure of human beta-galactosidase in complex with galactose

Structural highlights

3thc is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

BGAL_HUMAN GM1 gangliosidosis type 2;Mucopolysaccharidosis type 4B;GM1 gangliosidosis type 1;GM1 gangliosidosis type 3. GM1-gangliosidosis 1 (GM1G1) [MIM:230500: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. Note=The disease is caused by mutations affecting the gene represented in this entry.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] GM1-gangliosidosis 2 (GM1G2) [MIM:230600: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose-terminal oligosaccharides. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.[18] [19] [20] [21] [22] [23] [24] [25] [26] GM1-gangliosidosis 3 (GM1G3) [MIM:230650: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. Note=The disease is caused by mutations affecting the gene represented in this entry.[27] [28] [29] [30] [31] [32] [33] [34] [35] [36] Mucopolysaccharidosis 4B (MPS4B) [MIM:253010: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. Note=The disease is caused by mutations affecting the gene represented in this entry.[37] [38] [39] [40] [41] [42] [43]

Function

BGAL_HUMAN Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.[44] Isoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.[45]

Publication Abstract from PubMed

G(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme beta-d-galactosidase (beta-Gal), which lead to accumulations of the beta-Gal substrates, G(M1) ganglioside, and keratan sulfate. beta-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal beta-linked galactose residues. This study shows the crystal structures of human beta-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human beta-Gal is composed of a catalytic TIM barrel domain followed by beta-domain 1 and beta-domain 2. To gain structural insight into the molecular defects of beta-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed.

Crystal structure of human beta-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.,Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T J Biol Chem. 2012 Jan 13;287(3):1801-12. doi: 10.1074/jbc.M111.293795. Epub 2011 , Nov 28. PMID:22128166[46]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Oshima A, Yoshida K, Shimmoto M, Fukuhara Y, Sakuraba H, Suzuki Y. Human beta-galactosidase gene mutations in morquio B disease. Am J Hum Genet. 1991 Nov;49(5):1091-3. PMID:1928092
  2. ↑ Nishimoto J, Nanba E, Inui K, Okada S, Suzuki K. GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients. Am J Hum Genet. 1991 Sep;49(3):566-74. PMID:1909089
  3. ↑ Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y. Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases. Am J Hum Genet. 1991 Aug;49(2):435-42. PMID:1907800
  4. ↑ Mosna G, Fattore S, Tubiello G, Brocca S, Trubia M, Gianazza E, Gatti R, Danesino C, Minelli A, Piantanida M. A homozygous missense arginine to histidine substitution at position 482 of the beta-galactosidase in an Italian infantile GM1-gangliosidosis patient. Hum Genet. 1992 Nov;90(3):247-50. PMID:1487238
  5. ↑ Boustany RM, Qian WH, Suzuki K. Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American patients. Am J Hum Genet. 1993 Oct;53(4):881-8. PMID:8213816
  6. ↑ Paschke E, Milos I, Kreimer-Erlacher H, Hoefler G, Beck M, Hoeltzenbein M, Kleijer W, Levade T, Michelakakis H, Radeva B. Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B. Hum Genet. 2001 Aug;109(2):159-66. PMID:11511921
  7. ↑ Bagshaw RD, Zhang S, Hinek A, Skomorowski MA, Whelan D, Clarke JT, Callahan JW. Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B disease. Biochim Biophys Acta. 2002 Dec 12;1588(3):247-53. PMID:12393180
  8. ↑ Silva CM, Severini MH, Sopelsa A, Coelho JC, Zaha A, d'Azzo A, Giugliani R. Six novel beta-galactosidase gene mutations in Brazilian patients with GM1-gangliosidosis. Hum Mutat. 1999;13(5):401-9. PMID:10338095 doi:<401::AID-HUMU9>3.0.CO;2-N 10.1002/(SICI)1098-1004(1999)13:5<401::AID-HUMU9>3.0.CO;2-N
  9. ↑ Zhang S, Bagshaw R, Hilson W, Oho Y, Hinek A, Clarke JT, Callahan JW. Characterization of beta-galactosidase mutations Asp332-->Asn and Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1 gangliosidosis. Biochem J. 2000 Jun 15;348 Pt 3:621-32. PMID:10839995
  10. ↑ Morrone A, Bardelli T, Donati MA, Giorgi M, Di Rocco M, Gatti R, Parini R, Ricci R, Taddeucci G, D'Azzo A, Zammarchi E. beta-galactosidase gene mutations affecting the lysosomal enzyme and the elastin-binding protein in GM1-gangliosidosis patients with cardiac involvement. Hum Mutat. 2000;15(4):354-66. PMID:10737981 doi:<354::AID-HUMU8>3.0.CO;2-L 10.1002/(SICI)1098-1004(200004)15:4<354::AID-HUMU8>3.0.CO;2-L
  11. ↑ Georgiou T, Drousiotou A, Campos Y, Caciotti A, Sztriha L, Gururaj A, Ozand P, Zammarchi E, Morrone A, D'Azzo A. Four novel mutations in patients from the Middle East with the infantile form of GM1-gangliosidosis. Hum Mutat. 2004 Oct;24(4):352. PMID:15365997 doi:10.1002/humu.9279
  12. ↑ Caciotti A, Donati MA, Boneh A, d'Azzo A, Federico A, Parini R, Antuzzi D, Bardelli T, Nosi D, Kimonis V, Zammarchi E, Morrone A. Role of beta-galactosidase and elastin binding protein in lysosomal and nonlysosomal complexes of patients with GM1-gangliosidosis. Hum Mutat. 2005 Mar;25(3):285-92. PMID:15714521 doi:10.1002/humu.20147
  13. ↑ Gururaj A, Sztriha L, Hertecant J, Johansen JG, Georgiou T, Campos Y, Drousiotou A, d'Azzo A. Magnetic resonance imaging findings and novel mutations in GM1 gangliosidosis. J Child Neurol. 2005 Jan;20(1):57-60. PMID:15791924
  14. ↑ Santamaria R, Chabas A, Coll MJ, Miranda CS, Vilageliu L, Grinberg D. Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among gypsies. Hum Mutat. 2006 Oct;27(10):1060. PMID:16941474 doi:10.1002/humu.9451
  15. ↑ Tatano Y, Takeuchi N, Kuwahara J, Sakuraba H, Takahashi T, Takada G, Itoh K. Elastogenesis in cultured dermal fibroblasts from patients with lysosomal beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies. J Med Invest. 2006 Feb;53(1-2):103-12. PMID:16538002
  16. ↑ Santamaria R, Blanco M, Chabas A, Grinberg D, Vilageliu L. Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America. Clin Genet. 2007 Mar;71(3):273-9. PMID:17309651 doi:CGE767
  17. ↑ Hofer D, Paul K, Fantur K, Beck M, Burger F, Caillaud C, Fumic K, Ledvinova J, Lugowska A, Michelakakis H, Radeva B, Ramaswami U, Plecko B, Paschke E. GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase. Hum Mutat. 2009 Aug;30(8):1214-21. doi: 10.1002/humu.21031. PMID:19472408 doi:10.1002/humu.21031
  18. ↑ Nishimoto J, Nanba E, Inui K, Okada S, Suzuki K. GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients. Am J Hum Genet. 1991 Sep;49(3):566-74. PMID:1909089
  19. ↑ Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y. Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases. Am J Hum Genet. 1991 Aug;49(2):435-42. PMID:1907800
  20. ↑ Boustany RM, Qian WH, Suzuki K. Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American patients. Am J Hum Genet. 1993 Oct;53(4):881-8. PMID:8213816
  21. ↑ Morrone A, Bardelli T, Donati MA, Giorgi M, Di Rocco M, Gatti R, Parini R, Ricci R, Taddeucci G, D'Azzo A, Zammarchi E. beta-galactosidase gene mutations affecting the lysosomal enzyme and the elastin-binding protein in GM1-gangliosidosis patients with cardiac involvement. Hum Mutat. 2000;15(4):354-66. PMID:10737981 doi:<354::AID-HUMU8>3.0.CO;2-L 10.1002/(SICI)1098-1004(200004)15:4<354::AID-HUMU8>3.0.CO;2-L
  22. ↑ Caciotti A, Donati MA, Boneh A, d'Azzo A, Federico A, Parini R, Antuzzi D, Bardelli T, Nosi D, Kimonis V, Zammarchi E, Morrone A. Role of beta-galactosidase and elastin binding protein in lysosomal and nonlysosomal complexes of patients with GM1-gangliosidosis. Hum Mutat. 2005 Mar;25(3):285-92. PMID:15714521 doi:10.1002/humu.20147
  23. ↑ Santamaria R, Chabas A, Coll MJ, Miranda CS, Vilageliu L, Grinberg D. Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among gypsies. Hum Mutat. 2006 Oct;27(10):1060. PMID:16941474 doi:10.1002/humu.9451
  24. ↑ Santamaria R, Blanco M, Chabas A, Grinberg D, Vilageliu L. Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America. Clin Genet. 2007 Mar;71(3):273-9. PMID:17309651 doi:CGE767
  25. ↑ Hofer D, Paul K, Fantur K, Beck M, Burger F, Caillaud C, Fumic K, Ledvinova J, Lugowska A, Michelakakis H, Radeva B, Ramaswami U, Plecko B, Paschke E. GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase. Hum Mutat. 2009 Aug;30(8):1214-21. doi: 10.1002/humu.21031. PMID:19472408 doi:10.1002/humu.21031
  26. ↑ Caciotti A, Bardelli T, Cunningham J, D'Azzo A, Zammarchi E, Morrone A. Modulating action of the new polymorphism L436F detected in the GLB1 gene of a type-II GM1 gangliosidosis patient. Hum Genet. 2003 Jul;113(1):44-50. Epub 2003 Mar 19. PMID:12644936 doi:10.1007/s00439-003-0930-8
  27. ↑ Nishimoto J, Nanba E, Inui K, Okada S, Suzuki K. GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients. Am J Hum Genet. 1991 Sep;49(3):566-74. PMID:1909089
  28. ↑ Yoshida K, Oshima A, Shimmoto M, Fukuhara Y, Sakuraba H, Yanagisawa N, Suzuki Y. Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases. Am J Hum Genet. 1991 Aug;49(2):435-42. PMID:1907800
  29. ↑ Paschke E, Milos I, Kreimer-Erlacher H, Hoefler G, Beck M, Hoeltzenbein M, Kleijer W, Levade T, Michelakakis H, Radeva B. Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B. Hum Genet. 2001 Aug;109(2):159-66. PMID:11511921
  30. ↑ Santamaria R, Chabas A, Coll MJ, Miranda CS, Vilageliu L, Grinberg D. Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among gypsies. Hum Mutat. 2006 Oct;27(10):1060. PMID:16941474 doi:10.1002/humu.9451
  31. ↑ Santamaria R, Blanco M, Chabas A, Grinberg D, Vilageliu L. Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America. Clin Genet. 2007 Mar;71(3):273-9. PMID:17309651 doi:CGE767
  32. ↑ Hofer D, Paul K, Fantur K, Beck M, Burger F, Caillaud C, Fumic K, Ledvinova J, Lugowska A, Michelakakis H, Radeva B, Ramaswami U, Plecko B, Paschke E. GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase. Hum Mutat. 2009 Aug;30(8):1214-21. doi: 10.1002/humu.21031. PMID:19472408 doi:10.1002/humu.21031
  33. ↑ Chakraborty S, Rafi MA, Wenger DA. Mutations in the lysosomal beta-galactosidase gene that cause the adult form of GM1 gangliosidosis. Am J Hum Genet. 1994 Jun;54(6):1004-13. PMID:8198123
  34. ↑ Ishii N, Oohira T, Oshima A, Sakuraba H, Endo F, Matsuda I, Sukegawa K, Orii T, Suzuki Y. Clinical and molecular analysis of a Japanese boy with Morquio B disease. Clin Genet. 1995 Aug;48(2):103-8. PMID:7586649
  35. ↑ Paschke E, Milos I, Kreimer-Erlacher H, Hoefler G, Beck M, Hoeltzenbein M, Kleijer W, Levade T, Michelakakis H, Radeva B. Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B. Hum Genet. 2001 Aug;109(2):159-66. PMID:11511921
  36. ↑ Roze E, Paschke E, Lopez N, Eck T, Yoshida K, Maurel-Ollivier A, Doummar D, Caillaud C, Galanaud D, Billette de Villemeur T, Vidailhet M, Roubergue A. Dystonia and parkinsonism in GM1 type 3 gangliosidosis. Mov Disord. 2005 Oct;20(10):1366-9. PMID:15986423 doi:10.1002/mds.20593
  37. ↑ Oshima A, Yoshida K, Shimmoto M, Fukuhara Y, Sakuraba H, Suzuki Y. Human beta-galactosidase gene mutations in morquio B disease. Am J Hum Genet. 1991 Nov;49(5):1091-3. PMID:1928092
  38. ↑ Santamaria R, Chabas A, Coll MJ, Miranda CS, Vilageliu L, Grinberg D. Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among gypsies. Hum Mutat. 2006 Oct;27(10):1060. PMID:16941474 doi:10.1002/humu.9451
  39. ↑ Tatano Y, Takeuchi N, Kuwahara J, Sakuraba H, Takahashi T, Takada G, Itoh K. Elastogenesis in cultured dermal fibroblasts from patients with lysosomal beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies. J Med Invest. 2006 Feb;53(1-2):103-12. PMID:16538002
  40. ↑ Hofer D, Paul K, Fantur K, Beck M, Burger F, Caillaud C, Fumic K, Ledvinova J, Lugowska A, Michelakakis H, Radeva B, Ramaswami U, Plecko B, Paschke E. GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase. Hum Mutat. 2009 Aug;30(8):1214-21. doi: 10.1002/humu.21031. PMID:19472408 doi:10.1002/humu.21031
  41. ↑ Paschke E, Milos I, Kreimer-Erlacher H, Hoefler G, Beck M, Hoeltzenbein M, Kleijer W, Levade T, Michelakakis H, Radeva B. Mutation analyses in 17 patients with deficiency in acid beta-galactosidase: three novel point mutations and high correlation of mutation W273L with Morquio disease type B. Hum Genet. 2001 Aug;109(2):159-66. PMID:11511921
  42. ↑ Ishii N, Oohira T, Oshima A, Sakuraba H, Endo F, Matsuda I, Sukegawa K, Orii T, Suzuki Y. Clinical and molecular analysis of a Japanese boy with Morquio B disease. Clin Genet. 1995 Aug;48(2):103-8. PMID:7586649
  43. ↑ Bagshaw RD, Zhang S, Hinek A, Skomorowski MA, Whelan D, Clarke JT, Callahan JW. Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B disease. Biochim Biophys Acta. 2002 Dec 12;1588(3):247-53. PMID:12393180
  44. ↑ Hinek A. Biological roles of the non-integrin elastin/laminin receptor. Biol Chem. 1996 Jul-Aug;377(7-8):471-80. PMID:8922281
  45. ↑ Hinek A. Biological roles of the non-integrin elastin/laminin receptor. Biol Chem. 1996 Jul-Aug;377(7-8):471-80. PMID:8922281
  46. ↑ Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T. Crystal structure of human beta-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases. J Biol Chem. 2012 Jan 13;287(3):1801-12. doi: 10.1074/jbc.M111.293795. Epub 2011 , Nov 28. PMID:22128166 doi:10.1074/jbc.M111.293795

3thc, resolution 1.80Å

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