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==Crystal structure of Human fibrillar procollagen type III C- propeptide trimer==
==Crystal structure of Human fibrillar procollagen type III C- propeptide trimer==
<StructureSection load='4ak3' size='340' side='right' caption='[[4ak3]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='4ak3' size='340' side='right'caption='[[4ak3]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ak3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AK3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ak3]] is a 1 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=4AK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AK3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 3.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v53|2v53]], [[4ae2|4ae2]], [[4aej|4aej]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ak3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ak3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ak3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ak3 PDBsum]</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=4ak3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ak3 OCA], [https://pdbe.org/4ak3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ak3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ak3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ak3 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN]] Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:[http://omim.org/entry/130020 130020]]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.<ref>PMID:7833919</ref>  Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:[http://omim.org/entry/130050 130050]]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.<ref>PMID:1370809</ref> <ref>PMID:8411057</ref> <ref>PMID:2492273</ref> <ref>PMID:7749417</ref> <ref>PMID:1352273</ref> <ref>PMID:2808425</ref> <ref>PMID:1895316</ref> <ref>PMID:1357232</ref> <ref>PMID:1496983</ref> <ref>PMID:8098182</ref> [:]<ref>PMID:7912131</ref> <ref>PMID:8019562</ref> [:]<ref>PMID:8680408</ref> <ref>PMID:8884076</ref> <ref>PMID:9147870</ref> <ref>PMID:8664902</ref> <ref>PMID:8990011</ref> <ref>PMID:9036918</ref> <ref>PMID:9452103</ref> <ref>PMID:10923041</ref> <ref>PMID:10706896</ref> <ref>PMID:11168790</ref> <ref>PMID:12694234</ref> <ref>PMID:12786757</ref>  Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:[http://omim.org/entry/100070 100070]]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.<ref>PMID:8514866</ref> <ref>PMID:2243125</ref> <ref>PMID:2349939</ref>
[https://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN] Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:[https://omim.org/entry/130020 130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.<ref>PMID:7833919</ref>  Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:[https://omim.org/entry/130050 130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.<ref>PMID:1370809</ref> <ref>PMID:8411057</ref> <ref>PMID:2492273</ref> <ref>PMID:7749417</ref> <ref>PMID:1352273</ref> <ref>PMID:2808425</ref> <ref>PMID:1895316</ref> <ref>PMID:1357232</ref> <ref>PMID:1496983</ref> <ref>PMID:8098182</ref> [:]<ref>PMID:7912131</ref> <ref>PMID:8019562</ref> [:]<ref>PMID:8680408</ref> <ref>PMID:8884076</ref> <ref>PMID:9147870</ref> <ref>PMID:8664902</ref> <ref>PMID:8990011</ref> <ref>PMID:9036918</ref> <ref>PMID:9452103</ref> <ref>PMID:10923041</ref> <ref>PMID:10706896</ref> <ref>PMID:11168790</ref> <ref>PMID:12694234</ref> <ref>PMID:12786757</ref>  Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:[https://omim.org/entry/100070 100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.<ref>PMID:8514866</ref> <ref>PMID:2243125</ref> <ref>PMID:2349939</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN]] Collagen type III occurs in most soft connective tissues along with type I collagen.  
[https://www.uniprot.org/uniprot/CO3A1_HUMAN CO3A1_HUMAN] Collagen type III occurs in most soft connective tissues along with type I collagen.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 20:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4ak3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Collagen|Collagen]]
*[[Collagen 3D structures|Collagen 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Aghajari, N]]
[[Category: Large Structures]]
[[Category: Bourhis, J M]]
[[Category: Aghajari N]]
[[Category: Harlos, K]]
[[Category: Bourhis JM]]
[[Category: Hulmes, D J.S]]
[[Category: Harlos K]]
[[Category: Jones, E Y]]
[[Category: Hulmes DJS]]
[[Category: Mariano, N]]
[[Category: Jones EY]]
[[Category: Moali, C]]
[[Category: Mariano N]]
[[Category: Zhao, Y]]
[[Category: Moali C]]
[[Category: Extacellular matrix]]
[[Category: Zhao Y]]
[[Category: Fibrillar collagen]]
[[Category: Fibrosis]]
[[Category: Structural protein]]

Latest revision as of 14:28, 20 December 2023

Crystal structure of Human fibrillar procollagen type III C- propeptide trimerCrystal structure of Human fibrillar procollagen type III C- propeptide trimer

Structural highlights

4ak3 is a 1 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 3.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CO3A1_HUMAN Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.[1] Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:130050. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.[2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [:][12] [13] [:][14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:100070. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.[26] [27] [28]

Function

CO3A1_HUMAN Collagen type III occurs in most soft connective tissues along with type I collagen.

Publication Abstract from PubMed

The C propeptides of fibrillar procollagens have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. Mutations in C propeptides are associated with several, often lethal, genetic disorders affecting bone, cartilage, blood vessels and skin. Here we report the crystal structure of a C-propeptide domain from human procollagen III. It reveals an exquisite structural mechanism of chain recognition during intracellular trimerization of the procollagen molecule. It also gives insights into why some types of collagen consist of three identical polypeptide chains, whereas others do not. Finally, the data show striking correlations between the sites of numerous disease-related mutations in different C-propeptide domains and the degree of phenotype severity. The results have broad implications for understanding genetic disorders of connective tissues and designing new therapeutic strategies.

Structural basis of fibrillar collagen trimerization and related genetic disorders.,Bourhis JM, Mariano N, Zhao Y, Harlos K, Exposito JY, Jones EY, Moali C, Aghajari N, Hulmes DJ Nat Struct Mol Biol. 2012 Oct;19(10):1031-6. doi: 10.1038/nsmb.2389. Epub 2012, Sep 23. PMID:23001006[29]

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

See Also

References

  1. ↑ Narcisi P, Richards AJ, Ferguson SD, Pope FM. A family with Ehlers-Danlos syndrome type III/articular hypermobility syndrome has a glycine 637 to serine substitution in type III collagen. Hum Mol Genet. 1994 Sep;3(9):1617-20. PMID:7833919
  2. ↑ Richards AJ, Lloyd JC, Narcisi P, Ward PN, Nicholls AC, De Paepe A, Pope FM. A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV. Hum Genet. 1992 Jan;88(3):325-30. PMID:1370809
  3. ↑ Richards A, Narcisi P, Lloyd J, Ferguson C, Pope FM. The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV. J Med Genet. 1993 Aug;30(8):690-3. PMID:8411057
  4. ↑ Tromp G, Kuivaniemi H, Shikata H, Prockop DJ. A single base mutation that substitutes serine for glycine 790 of the alpha 1 (III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV. J Biol Chem. 1989 Jan 25;264(3):1349-52. PMID:2492273
  5. ↑ Tromp G, De Paepe A, Nuytinck L, Madhatheri S, Kuivaniemi H. Substitution of valine for glycine 793 in type III procollagen in Ehlers-Danlos syndrome type IV. Hum Mutat. 1995;5(2):179-81. PMID:7749417 doi:http://dx.doi.org/10.1002/humu.1380050213
  6. ↑ Richards AJ, Ward PN, Narcisi P, Nicholls AC, Lloyd JC, Pope FM. A single base mutation in the gene for type III collagen (COL3A1) converts glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type IV. An unaffected family member is mosaic for the mutation. Hum Genet. 1992 Jun;89(4):414-8. PMID:1352273
  7. ↑ Tromp G, Kuivaniemi H, Stolle C, Pope FM, Prockop DJ. Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV. J Biol Chem. 1989 Nov 15;264(32):19313-7. PMID:2808425
  8. ↑ Richards AJ, Lloyd JC, Ward PN, De Paepe A, Narcisi P, Pope FM. Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV. J Med Genet. 1991 Jul;28(7):458-63. PMID:1895316
  9. ↑ Johnson PH, Richards AJ, Pope FM, Hopkinson DA. A COL3A1 glycine 1006 to glutamic acid substitution in a patient with Ehlers-Danlos syndrome type IV detected by denaturing gradient gel electrophoresis. J Inherit Metab Dis. 1992;15(3):426-30. PMID:1357232
  10. ↑ Kontusaari S, Tromp G, Kuivaniemi H, Stolle C, Pope FM, Prockop DJ. Substitution of aspartate for glycine 1018 in the type III procollagen (COL3A1) gene causes type IV Ehlers-Danlos syndrome: the mutated allele is present in most blood leukocytes of the asymptomatic and mosaic mother. Am J Hum Genet. 1992 Sep;51(3):497-507. PMID:1496983
  11. ↑ Narcisi P, Wu Y, Tromp G, Earley JJ, Richards AJ, Pope FM, Kuivaniemi H. Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV. Am J Med Genet. 1993 May 15;46(3):278-83. PMID:8098182 doi:http://dx.doi.org/10.1002/ajmg.1320460308
  12. ↑ Madhatheri SL, Tromp G, Gustavson KH, Kuivaniemi H. Substitution of glutamic acid for glycine 589 in the triple-helical domain of type III procollagen (COL3A1) in a family with variable phenotype of the Ehlers-Danlos syndrome type IV. Hum Mol Genet. 1994 Mar;3(3):511-2. PMID:7912131
  13. ↑ Nuytinck L, De Paepe A, Renard JP, Adriaens F, Leroy J. Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene detects a mutation that results in the substitution of glycine 1009 to valine and causes severe Ehlers-Danlos syndrome type IV. Hum Mutat. 1994;3(3):268-74. PMID:8019562 doi:http://dx.doi.org/10.1002/humu.1380030315
  14. ↑ Johnson PH, Richards AJ, Lloyd JC, Pope FM, Hopkinson DA. Efficient strategy for the detection of mutations in acrogeric Ehlers-Danlos syndrome type IV. Hum Mutat. 1995;6(4):336-42. PMID:8680408 doi:10.1002/humu.1380060408
  15. ↑ Mackay K, Raghunath M, Superti-Furga A, Steinmann B, Dalgleish R. Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and Gly1003Asp substitutions in collagen III: clinical features, biochemical screening, and molecular confirmation. Clin Genet. 1996 Jun;49(6):286-95. PMID:8884076
  16. ↑ McGrory J, Weksberg R, Thorner P, Cole WG. Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due to the substitution of glycine 934 by glutamic acid in the triple helical domain of type III collagen. Clin Genet. 1996 Dec;50(6):442-5. PMID:9147870
  17. ↑ McGrory J, Costa T, Cole WG. A novel G499D substitution in the alpha 1(III) chain of type III collagen produces variable forms of Ehlers-Danlos syndrome type IV. Hum Mutat. 1996;7(1):59-60. PMID:8664902 doi:<59::AID-HUMU8>3.0.CO;2-K 10.1002/(SICI)1098-1004(1996)7:1<59::AID-HUMU8>3.0.CO;2-K
  18. ↑ Anderson DW, Thakker-Varia S, Tromp G, Kuivaniemi H, Stolle CA. A glycine (415)-to-serine substitution results in impaired secretion and decreased thermal stability of type III procollagen in a patient with Ehlers-Danlos syndrome type IV. Hum Mutat. 1997;9(1):62-3. PMID:8990011 doi:<62::AID-HUMU11>3.0.CO;2-N 10.1002/(SICI)1098-1004(1997)9:1<62::AID-HUMU11>3.0.CO;2-N
  19. ↑ Smith LT, Schwarze U, Goldstein J, Byers PH. Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis. J Invest Dermatol. 1997 Mar;108(3):241-7. PMID:9036918
  20. ↑ Bateman JF, Chiodo AA, Weng YM, Chan D, Haan E. A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos syndrome type IV. Hum Mutat. 1998;Suppl 1:S257-9. PMID:9452103
  21. ↑ Giunta C, Steinmann B. Characterization of 11 new mutations in COL3A1 of individuals with Ehlers-Danlos syndrome type IV: preliminary comparison of RNase cleavage, EMC and DHPLC assays. Hum Mutat. 2000 Aug;16(2):176-7. PMID:10923041 doi:<176::AID-HUMU12>3.0.CO;2-E 10.1002/1098-1004(200008)16:2<176::AID-HUMU12>3.0.CO;2-E
  22. ↑ Pepin M, Schwarze U, Superti-Furga A, Byers PH. Clinical and genetic features of Ehlers-Danlos syndrome type IV, the vascular type. N Engl J Med. 2000 Mar 9;342(10):673-80. PMID:10706896
  23. ↑ Nishiyama Y, Nejima J, Watanabe A, Kotani E, Sakai N, Hatamochi A, Shinkai H, Kiuchi K, Tamura K, Shimada T, Takano T, Katayama Y. Ehlers-Danlos syndrome type IV with a unique point mutation in COL3A1 and familial phenotype of myocardial infarction without organic coronary stenosis. J Intern Med. 2001 Jan;249(1):103-8. PMID:11168790
  24. ↑ Kroes HY, Pals G, van Essen AJ. Ehlers-Danlos syndrome type IV: unusual congenital anomalies in a mother and son with a COL3A1 mutation and a normal collagen III protein profile. Clin Genet. 2003 Mar;63(3):224-7. PMID:12694234
  25. ↑ Palmeri S, Mari F, Meloni I, Malandrini A, Ariani F, Villanova M, Pompilio A, Schwarze U, Byers PH, Renieri A. Neurological presentation of Ehlers-Danlos syndrome type IV in a family with parental mosaicism. Clin Genet. 2003 Jun;63(6):510-5. PMID:12786757
  26. ↑ Tromp G, Wu Y, Prockop DJ, Madhatheri SL, Kleinert C, Earley JJ, Zhuang J, Norrgard O, Darling RC, Abbott WM, et al.. Sequencing of cDNA from 50 unrelated patients reveals that mutations in the triple-helical domain of type III procollagen are an infrequent cause of aortic aneurysms. J Clin Invest. 1993 Jun;91(6):2539-45. PMID:8514866 doi:http://dx.doi.org/10.1172/JCI116490
  27. ↑ Kontusaari S, Tromp G, Kuivaniemi H, Romanic AM, Prockop DJ. A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms. J Clin Invest. 1990 Nov;86(5):1465-73. PMID:2243125 doi:http://dx.doi.org/10.1172/JCI114863
  28. ↑ Kontusaari S, Tromp G, Kuivaniemi H, Ladda RL, Prockop DJ. Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III procollagen gene (COL3A1) in a family having aortic aneurysms and easy bruisability: phenotypic overlap between familial arterial aneurysms and Ehlers-Danlos syndrome type IV. Am J Hum Genet. 1990 Jul;47(1):112-20. PMID:2349939
  29. ↑ Bourhis JM, Mariano N, Zhao Y, Harlos K, Exposito JY, Jones EY, Moali C, Aghajari N, Hulmes DJ. Structural basis of fibrillar collagen trimerization and related genetic disorders. Nat Struct Mol Biol. 2012 Oct;19(10):1031-6. doi: 10.1038/nsmb.2389. Epub 2012, Sep 23. PMID:23001006 doi:http://dx.doi.org/10.1038/nsmb.2389

4ak3, resolution 3.50Å

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