7v0s: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[7v0s]] 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=7V0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0S FirstGlance]. <br>
-</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></td></tr>
+</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>
+<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></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=7v0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0s OCA], [https://pdbe.org/7v0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0s RCSB], [https://www.ebi.ac.uk/pdbsum/7v0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0s ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[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.
+[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.
 == Function ==
-[[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.
+[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.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
+==See Also==
+*[[Ankyrin 3D structures|Ankyrin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7v0s" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>