7tth
From Proteopedia
(Difference between revisions)
Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7tth]] is a 2 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=7TTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTH FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tth]] is a 2 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=7TTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TTH FirstGlance]. <br> | ||
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 3.25Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <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=7tth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tth OCA], [https://pdbe.org/7tth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tth RCSB], [https://www.ebi.ac.uk/pdbsum/7tth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tth ProSAT]</span></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=7tth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tth OCA], [https://pdbe.org/7tth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tth RCSB], [https://www.ebi.ac.uk/pdbsum/7tth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tth ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/S12A4_HUMAN S12A4_HUMAN] Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity). Isoform 4 has no transport activity. | |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cation-chloride cotransporters (CCCs) catalyze electroneutral symport of Cl(-) with Na(+) and/or K(+) across membranes. CCCs are fundamental in cell volume homeostasis, transepithelia ion movement, maintenance of intracellular Cl(-) concentration, and neuronal excitability. Here, we present a cryoelectron microscopy structure of human K(+)-Cl(-) cotransporter (KCC)1 bound with the VU0463271 inhibitor in an outward-open state. In contrast to many other amino acid-polyamine-organocation transporter cousins, our first outward-open CCC structure reveals that opening the KCC1 extracellular ion permeation path does not involve hinge-bending motions of the transmembrane (TM) 1 and TM6 half-helices. Instead, rocking of TM3 and TM8, together with displacements of TM4, TM9, and a conserved intracellular loop 1 helix, underlie alternate opening and closing of extracellular and cytoplasmic vestibules. We show that KCC1 intriguingly exists in one of two distinct dimeric states via different intersubunit interfaces. Our studies provide a blueprint for understanding the mechanisms of CCCs and their inhibition by small molecule compounds. | ||
+ | |||
+ | Structure of the human cation-chloride cotransport KCC1 in an outward-open state.,Zhao Y, Shen J, Wang Q, Ruiz Munevar MJ, Vidossich P, De Vivo M, Zhou M, Cao E Proc Natl Acad Sci U S A. 2022 Jul 5;119(27):e2109083119. doi: , 10.1073/pnas.2109083119. Epub 2022 Jun 27. PMID:35759661<ref>PMID:35759661</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7tth" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Solute carrier family 12 3D structures|Solute carrier family 12 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Human potassium-chloride cotransporter 1 in inward-open state
|