7d14: Difference between revisions

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New page: '''Unreleased structure''' The entry 7d14 is ON HOLD Authors: Sensen, Z. Description: mouse KCC2 Category: Unreleased Structures Category: Sensen, Z
 
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'''Unreleased structure'''


The entry 7d14 is ON HOLD
==Mouse KCC2==
<StructureSection load='7d14' size='340' side='right'caption='[[7d14]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D14 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#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=7d14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d14 OCA], [https://pdbe.org/7d14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d14 RCSB], [https://www.ebi.ac.uk/pdbsum/7d14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d14 ProSAT]</span></td></tr>
</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.


Authors: Sensen, Z.
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>


Description: mouse KCC2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Sensen, Z]]
<div class="pdbe-citations 7d14" 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__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yang M]]
[[Category: Zhang S]]

Latest revision as of 22:31, 29 May 2024

Mouse KCC2Mouse KCC2

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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. The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. Commun Biol. 2021 Feb 17;4(1):226. PMID:33597714 doi:10.1038/s42003-021-01750-w

7d14, resolution 3.80Å

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