8csw

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Current revision (09:40, 14 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8csw]] 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=8CSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSW FirstGlance]. <br>
<table><tr><td colspan='2'>[[8csw]] 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=8CSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSW FirstGlance]. <br>
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</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=8csw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csw OCA], [https://pdbe.org/8csw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csw RCSB], [https://www.ebi.ac.uk/pdbsum/8csw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csw ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8csw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csw OCA], [https://pdbe.org/8csw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csw RCSB], [https://www.ebi.ac.uk/pdbsum/8csw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csw ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Hereditary spherocytosis. The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN] Hereditary spherocytosis. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.
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[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN] Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.
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Architecture of the human erythrocyte ankyrin-1 complex.,Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865<ref>PMID:35835865</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8csw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Local refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complex

PDB ID 8csw

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