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7v0k

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'''Unreleased structure'''
 
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The entry 7v0k is ON HOLD until Paper Publication
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==Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map)==
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<StructureSection load='7v0k' size='340' side='right'caption='[[7v0k]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7v0k]] is a 10 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=7V0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP:Digitonin'>AJP</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PIO:[(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-PHOSPHORYL]OXY-PROPYL]+OCTANOATE'>PIO</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</scene></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=7v0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0k OCA], [https://pdbe.org/7v0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0k RCSB], [https://www.ebi.ac.uk/pdbsum/7v0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0k ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[https://www.uniprot.org/uniprot/RHCE_HUMAN RHCE_HUMAN]] Rh deficiency syndrome. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[[https://www.uniprot.org/uniprot/RHCE_HUMAN RHCE_HUMAN]] May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
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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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Authors:
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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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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7v0k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cali T]]
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[[Category: Clarke OB]]
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[[Category: Johnston JD]]
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[[Category: Kim K]]
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[[Category: Noble AJ]]
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[[Category: Vallese F]]
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[[Category: Yen LY]]

Current revision

Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map)

PDB ID 7v0k

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