8csx
From Proteopedia
(Difference between revisions)
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<table><tr><td colspan='2'>[[8csx]] is a 3 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=8CSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSX FirstGlance]. <br> | <table><tr><td colspan='2'>[[8csx]] is a 3 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=8CSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CSX FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.4Å</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]] 2.4Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP:(25R)-2beta,15alpha-dihydroxy-5beta,8alpha,10alpha,14beta,17beta-spirostan-3alpha-yl+beta-D-glucopyranosyl-(1- 3)-beta-D-galactopyranosyl-(1- 2)-[beta-D-xylopyranosyl-(1- 3)]-beta-D-glucopyranosyl-(1- 4)-beta-D-galactopyranoside'>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=8csx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csx OCA], [https://pdbe.org/8csx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csx RCSB], [https://www.ebi.ac.uk/pdbsum/8csx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csx 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=8csx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8csx OCA], [https://pdbe.org/8csx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8csx RCSB], [https://www.ebi.ac.uk/pdbsum/8csx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8csx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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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. | [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 == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/RHCE_HUMAN RHCE_HUMAN] | + | [https://www.uniprot.org/uniprot/RHCE_HUMAN RHCE_HUMAN] Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Mediates the primary membrane attachment site for ANK1 when associated with RHAG (PubMed:35835865). May participate in the ammonium and carbon dioxide transport through the heterotrimer form (Probable).<ref>PMID:35835865</ref> |
| + | <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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8csx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Local refinement of RhAG/CE trimer in class 2 of erythrocyte ankyrin-1 complex
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Categories: Homo sapiens | Large Structures | Cali T | Clarke OB | Johnston JD | Kim K | Noble AJ | Vallese F | Yen LY
