8ct2
From Proteopedia
(Difference between revisions)
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==Local refinement of AQP1 tetramer (C1; refinement mask included D1 of protein 4.2 and Ankyrin-1 AR1-5) in Class 2 of erythrocyte ankyrin-1 complex== | ==Local refinement of AQP1 tetramer (C1; refinement mask included D1 of protein 4.2 and Ankyrin-1 AR1-5) in Class 2 of erythrocyte ankyrin-1 complex== | ||
| - | <StructureSection load='8ct2' size='340' side='right'caption='[[8ct2]]' scene=''> | + | <StructureSection load='8ct2' size='340' side='right'caption='[[8ct2]], [[Resolution|resolution]] 3.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CT2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8ct2]] 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=8CT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CT2 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=8ct2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ct2 OCA], [https://pdbe.org/8ct2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ct2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ct2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ct2 ProSAT]</span></td></tr> | + | </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></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=P1L:S-PALMITOYL-L-CYSTEINE'>P1L</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=8ct2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ct2 OCA], [https://pdbe.org/8ct2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ct2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ct2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ct2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/AQP1_HUMAN AQP1_HUMAN]] Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.<ref>PMID:1373524</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 8ct2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cali T]] | + | [[Category: Cali, T]] |
| - | [[Category: Clarke | + | [[Category: Clarke, O B]] |
| - | [[Category: Johnston | + | [[Category: Johnston, J D]] |
| - | [[Category: Kim K]] | + | [[Category: Kim, K]] |
| - | [[Category: Noble | + | [[Category: Noble, A J]] |
| - | [[Category: Vallese F]] | + | [[Category: Vallese, F]] |
| - | [[Category: Yen | + | [[Category: Yen, L Y]] |
| + | [[Category: Anion exchange]] | ||
| + | [[Category: Erythrocyte]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Transport protein-structural protein complex]] | ||
Revision as of 18:21, 27 July 2022
Local refinement of AQP1 tetramer (C1; refinement mask included D1 of protein 4.2 and Ankyrin-1 AR1-5) in Class 2 of erythrocyte ankyrin-1 complex
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