7v0q: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7v0q]] is a 1 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=7V0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[7v0q]] is a 1 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=7V0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V0Q FirstGlance]. <br>
</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=7v0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0q OCA], [https://pdbe.org/7v0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0q RCSB], [https://www.ebi.ac.uk/pdbsum/7v0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0q ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7v0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v0q OCA], [https://pdbe.org/7v0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v0q RCSB], [https://www.ebi.ac.uk/pdbsum/7v0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v0q ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Hereditary spherocytosis. The disease is caused by variants affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN] Hereditary spherocytosis. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN]] Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.  
[https://www.uniprot.org/uniprot/EPB42_HUMAN EPB42_HUMAN] Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v0q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cali, T]]
[[Category: Cali T]]
[[Category: Clarke, O B]]
[[Category: Clarke OB]]
[[Category: Johnston, J D]]
[[Category: Johnston JD]]
[[Category: Kim, K]]
[[Category: Kim K]]
[[Category: Noble, A J]]
[[Category: Noble AJ]]
[[Category: Vallese, F]]
[[Category: Vallese F]]
[[Category: Yen, L Y]]
[[Category: Yen LY]]
[[Category: Ankyrin complex]]
[[Category: Erythrocyte]]
[[Category: Membrane protein]]
[[Category: Structural protein]]

Latest revision as of 09:39, 14 February 2024

Local refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complex

7v0q, resolution 2.50Å

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