1s35: Difference between revisions

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<StructureSection load='1s35' size='340' side='right'caption='[[1s35]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1s35' size='340' side='right'caption='[[1s35]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1s35]] is a 1 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=1S35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S35 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1s35]] 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=1S35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S35 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPTB, SPTB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1s35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s35 OCA], [https://pdbe.org/1s35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s35 RCSB], [https://www.ebi.ac.uk/pdbsum/1s35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s35 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=1s35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s35 OCA], [https://pdbe.org/1s35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s35 RCSB], [https://www.ebi.ac.uk/pdbsum/1s35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s35 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]]. EL3 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref>  Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.  
[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]. EL3 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref>  Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.  
[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s35 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s35 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.
Structural insights into the stability and flexibility of unusual erythroid spectrin repeats.,Kusunoki H, MacDonald RI, Mondragon A Structure. 2004 Apr;12(4):645-56. PMID:15062087<ref>PMID:15062087</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1s35" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Spectrin|Spectrin]]
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kusunoki, H]]
[[Category: Kusunoki H]]
[[Category: MacDonald, R I]]
[[Category: MacDonald RI]]
[[Category: Mondragon, A]]
[[Category: Mondragon A]]
[[Category: 3-helix coiled-coil]]
[[Category: Alpha helical linker region]]
[[Category: Beta spectrin]]
[[Category: Structural protein]]
[[Category: Two repeats of spectrin]]

Latest revision as of 11:28, 14 February 2024

Crystal Structure of Repeats 8 and 9 of Human Erythroid SpectrinCrystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin

Structural highlights

1s35 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 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

SPTB1_HUMAN Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:182870. EL3 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.[1] [2] [3] [4] Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:182870; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.

Function

SPTB1_HUMAN Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Sahr KE, Coetzer TL, Moy LS, Derick LH, Chishti AH, Jarolim P, Lorenzo F, Miraglia del Giudice E, Iolascon A, Gallanello R, et al.. Spectrin cagliari. an Ala-->Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. J Biol Chem. 1993 Oct 25;268(30):22656-62. PMID:8226774
  2. ↑ Gallagher PG, Weed SA, Tse WT, Benoit L, Morrow JS, Marchesi SL, Mohandas N, Forget BG. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene. J Clin Invest. 1995 Mar;95(3):1174-82. PMID:7883966 doi:http://dx.doi.org/10.1172/JCI117766
  3. ↑ Parquet N, Devaux I, Boulanger L, Galand C, Boivin P, Lecomte MC, Dhermy D, Garbarz M. Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: further support for a triple-stranded folding unit model of the spectrin heterodimer contact site. Blood. 1994 Jul 1;84(1):303-8. PMID:8018926
  4. ↑ Tse WT, Lecomte MC, Costa FF, Garbarz M, Feo C, Boivin P, Dhermy D, Forget BG. Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association. J Clin Invest. 1990 Sep;86(3):909-16. PMID:1975598 doi:http://dx.doi.org/10.1172/JCI114792

1s35, resolution 2.40Å

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