7d10: Difference between revisions
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==Human NKCC1== | ==Human NKCC1== | ||
<StructureSection load='7d10' size='340' side='right'caption='[[7d10]]' scene=''> | <StructureSection load='7d10' size='340' side='right'caption='[[7d10]], [[Resolution|resolution]] 3.52Å' 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=7D10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D10 FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D10 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=7d10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d10 OCA], [https://pdbe.org/7d10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d10 RCSB], [https://www.ebi.ac.uk/pdbsum/7d10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d10 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]] 3.52Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=7d10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d10 OCA], [https://pdbe.org/7d10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d10 RCSB], [https://www.ebi.ac.uk/pdbsum/7d10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d10 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NKCC and KCC transporters mediate coupled transport of Na(+)+K(+)+Cl(-) and K(+)+Cl(-) across the plasma membrane, thus regulating cell Cl(-) concentration and cell volume and playing critical roles in transepithelial salt and water transport and in neuronal excitability. The function of these transporters has been intensively studied, but a mechanistic understanding has awaited structural studies of the transporters. Here, we present the cryo-electron microscopy (cryo-EM) structures of the two neuronal cation-chloride cotransporters human NKCC1 (SLC12A2) and mouse KCC2 (SLC12A5), along with computational analysis and functional characterization. These structures highlight essential residues in ion transport and allow us to propose mechanisms by which phosphorylation regulates transport activity. | |||
The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.,Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M Commun Biol. 2021 Feb 17;4(1):226. doi: 10.1038/s42003-021-01750-w. PMID:33597714<ref>PMID:33597714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7d10" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Solute carrier family 12 3D structures|Solute carrier family 12 3D structures]] | |||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 22:31, 29 May 2024
Human NKCC1Human NKCC1
Structural highlights
Publication Abstract from PubMedNKCC and KCC transporters mediate coupled transport of Na(+)+K(+)+Cl(-) and K(+)+Cl(-) across the plasma membrane, thus regulating cell Cl(-) concentration and cell volume and playing critical roles in transepithelial salt and water transport and in neuronal excitability. The function of these transporters has been intensively studied, but a mechanistic understanding has awaited structural studies of the transporters. Here, we present the cryo-electron microscopy (cryo-EM) structures of the two neuronal cation-chloride cotransporters human NKCC1 (SLC12A2) and mouse KCC2 (SLC12A5), along with computational analysis and functional characterization. These structures highlight essential residues in ion transport and allow us to propose mechanisms by which phosphorylation regulates transport activity. The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.,Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M Commun Biol. 2021 Feb 17;4(1):226. doi: 10.1038/s42003-021-01750-w. PMID:33597714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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