7d8z: Difference between revisions
New page: '''Unreleased structure''' The entry 7d8z is ON HOLD Authors: Description: Category: Unreleased Structures |
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==human potassium-chloride co-transporter KCC2== | |||
<StructureSection load='7d8z' size='340' side='right'caption='[[7d8z]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D8Z 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]] 3.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7d8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d8z OCA], [https://pdbe.org/7d8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d8z RCSB], [https://www.ebi.ac.uk/pdbsum/7d8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d8z ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Potassium-chloride cotransporters KCC1 to KCC4 mediate the coupled export of potassium and chloride across the plasma membrane and play important roles in cell volume regulation, auditory system function, and gamma-aminobutyric acid (GABA) and glycine-mediated inhibitory neurotransmission. Here, we present 2.9- to 3.6-A resolution structures of full-length human KCC2, KCC3, and KCC4. All three KCCs adopt a similar overall architecture, a domain-swap dimeric assembly, and an inward-facing conformation. The structural and functional studies reveal that one unexpected N-terminal peptide binds at the cytosolic facing cavity and locks KCC2 and KCC4 at an autoinhibition state. The C-terminal domain (CTD) directly interacts with the N-terminal inhibitory peptide, and the relative motions between the CTD and the transmembrane domain (TMD) suggest that CTD regulates KCCs' activities by adjusting the autoinhibitory effect. These structures provide the first glimpse of full-length structures of KCCs and an autoinhibition mechanism among the amino acid-polyamine-organocation transporter superfamily. | |||
Structures and an activation mechanism of human potassium-chloride cotransporters.,Xie Y, Chang S, Zhao C, Wang F, Liu S, Wang J, Delpire E, Ye S, Guo J Sci Adv. 2020 Dec 11;6(50). pii: 6/50/eabc5883. doi: 10.1126/sciadv.abc5883., Print 2020 Dec. PMID:33310850<ref>PMID:33310850</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7d8z" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chang S]] | |||
[[Category: Guo J]] | |||
[[Category: Xie Y]] | |||
[[Category: Ye S]] | |||
[[Category: Zhao C]] | |||
Latest revision as of 12:23, 9 October 2024
human potassium-chloride co-transporter KCC2human potassium-chloride co-transporter KCC2
Structural highlights
Publication Abstract from PubMedPotassium-chloride cotransporters KCC1 to KCC4 mediate the coupled export of potassium and chloride across the plasma membrane and play important roles in cell volume regulation, auditory system function, and gamma-aminobutyric acid (GABA) and glycine-mediated inhibitory neurotransmission. Here, we present 2.9- to 3.6-A resolution structures of full-length human KCC2, KCC3, and KCC4. All three KCCs adopt a similar overall architecture, a domain-swap dimeric assembly, and an inward-facing conformation. The structural and functional studies reveal that one unexpected N-terminal peptide binds at the cytosolic facing cavity and locks KCC2 and KCC4 at an autoinhibition state. The C-terminal domain (CTD) directly interacts with the N-terminal inhibitory peptide, and the relative motions between the CTD and the transmembrane domain (TMD) suggest that CTD regulates KCCs' activities by adjusting the autoinhibitory effect. These structures provide the first glimpse of full-length structures of KCCs and an autoinhibition mechanism among the amino acid-polyamine-organocation transporter superfamily. Structures and an activation mechanism of human potassium-chloride cotransporters.,Xie Y, Chang S, Zhao C, Wang F, Liu S, Wang J, Delpire E, Ye S, Guo J Sci Adv. 2020 Dec 11;6(50). pii: 6/50/eabc5883. doi: 10.1126/sciadv.abc5883., Print 2020 Dec. PMID:33310850[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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