View source for 6pzt


==cryo-EM structure of human NKCC1==
<StructureSection load='6pzt' size='340' side='right'caption='[[6pzt]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pzt]] 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=6PZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PZT 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]] 3.46&#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=6pzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pzt OCA], [https://pdbe.org/6pzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pzt RCSB], [https://www.ebi.ac.uk/pdbsum/6pzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pzt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S12A2_HUMAN S12A2_HUMAN] Electrically silent transporter system. Mediates sodium and chloride reabsorption. Plays a vital role in the regulation of ionic balance and cell volume.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The secondary active cation-chloride cotransporters (CCCs) utilize the existing Na(+) and/or K(+) gradients to move Cl(-) into or out of cells. NKCC1 is an intensively studied member of the CCC family and plays fundamental roles in regulating trans-epithelial ion movement, cell volume, chloride homeostasis and neuronal excitability. Here, we report a cryo-EM structure of human NKCC1 captured in a partially loaded, inward-open state. NKCC1 assembles into a dimer, with the first ten transmembrane (TM) helices harboring the transport core and TM11-TM12 helices lining the dimer interface. TM1 and TM6 helices break alpha-helical geometry halfway across the lipid bilayer where ion binding sites are organized around these discontinuous regions. NKCC1 may harbor multiple extracellular entryways and intracellular exits, raising the possibility that K(+), Na(+), and Cl(-) ions may traverse along their own routes for translocation. NKCC1 structure provides a blueprint for further probing structure-function relationships of NKCC1 and other CCCs.

Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy.,Yang X, Wang Q, Cao E Nat Commun. 2020 Feb 21;11(1):1016. doi: 10.1038/s41467-020-14790-3. PMID:32081947<ref>PMID:32081947</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pzt" 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: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cao E]]
[[Category: Wang Q]]
[[Category: Yang X]]