7v0k: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJP: | </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:(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>, <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> | |||
<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> | <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> | ||
</table> | </table> | ||
== Disease == | == 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. | |||
== Function == | == Function == | ||
[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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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> | 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> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7v0k" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7v0k" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ankyrin 3D structures|Ankyrin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||