8crt: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8crt]] is a 8 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=8CRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CRT FirstGlance]. <br> | <table><tr><td colspan='2'>[[8crt]] is a 8 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=8CRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CRT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8crt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8crt OCA], [https://pdbe.org/8crt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8crt RCSB], [https://www.ebi.ac.uk/pdbsum/8crt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8crt 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=8crt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8crt OCA], [https://pdbe.org/8crt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8crt RCSB], [https://www.ebi.ac.uk/pdbsum/8crt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8crt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[https://www.uniprot.org/uniprot/RHAG_HUMAN RHAG_HUMAN] Rh deficiency syndrome;Overhydrated hereditary stomatocytosis. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RHAG_HUMAN RHAG_HUMAN] Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Heterotrimer with RHCE (RHAG)2(RHCE), that transports ammonium and its related derivative methylammonium, in both neutral and ionic forms, across the erythrocyte membrane (PubMed:11062476, PubMed:11861637, PubMed:15572441, PubMed:15856280, PubMed:19273840, PubMed:21849667, PubMed:22012326, PubMed:24077989, PubMed:26354748). The transport of NH4(+) is electrogenic and masks the NH3 transport (PubMed:26354748). Also, may act as a CO2 channel (PubMed:17712059, PubMed:19273840, PubMed:24077989). In vitro, leaks monovalent cations (PubMed:18931342, PubMed:21849667). Moreover in erythrocyte, regulates RHD membrane expression (PubMed:12130520) and is associated with rhesus blood group antigen expression (PubMed:12130520, PubMed:19744193).<ref>PMID:11062476</ref> <ref>PMID:11861637</ref> <ref>PMID:12130520</ref> <ref>PMID:15572441</ref> <ref>PMID:15856280</ref> <ref>PMID:17712059</ref> <ref>PMID:18931342</ref> <ref>PMID:19273840</ref> <ref>PMID:19744193</ref> <ref>PMID:21849667</ref> <ref>PMID:22012326</ref> <ref>PMID:24077989</ref> <ref>PMID:26354748</ref> <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 8crt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8crt" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Anion exchange protein 3D structures|Anion exchange protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||