6npj

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<SX load='6npj' size='340' side='right' viewer='molstar' caption='[[6npj]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<SX load='6npj' size='340' side='right' viewer='molstar' caption='[[6npj]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6npj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NPJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6npj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NPJ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">slc12a2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6npj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6npj OCA], [http://pdbe.org/6npj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6npj RCSB], [http://www.ebi.ac.uk/pdbsum/6npj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6npj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6npj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6npj OCA], [https://pdbe.org/6npj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6npj RCSB], [https://www.ebi.ac.uk/pdbsum/6npj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6npj ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/S12A2_DANRE S12A2_DANRE] Cation-chloride cotransporter which mediates the electroneutral transport of chloride, potassium and/or sodium ions across the membrane (PubMed:31367042). Plays a vital role in the regulation of ionic balance and cell volume (PubMed:31367042). Important for maintenance of endolymph volume in the otic vesicle, probably by regulating ion homeostasis (PubMed:19633174). Also plays a role in normal development of the swim bladder (PubMed:19633174).<ref>PMID:19633174</ref> <ref>PMID:31367042</ref>
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Cation-chloride cotransporters (CCCs) mediate the electroneutral transport of chloride, potassium and/or sodium across the membrane. They have critical roles in regulating cell volume, controlling ion absorption and secretion across epithelia, and maintaining intracellular chloride homeostasis. These transporters are primary targets for some of the most commonly prescribed drugs. Here we determined the cryo-electron microscopy structure of the Na-K-Cl cotransporter NKCC1, an extensively studied member of the CCC family, from Danio rerio. The structure defines the architecture of this protein family and reveals how cytosolic and transmembrane domains are strategically positioned for communication. Structural analyses, functional characterizations and computational studies reveal the ion-translocation pathway, ion-binding sites and key residues for transport activity. These results provide insights into ion selectivity, coupling and translocation, and establish a framework for understanding the physiological functions of CCCs and interpreting disease-related mutations.
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Structure and mechanism of the cation-chloride cotransporter NKCC1.,Chew TA, Orlando BJ, Zhang J, Latorraca NR, Wang A, Hollingsworth SA, Chen DH, Dror RO, Liao M, Feng L Nature. 2019 Jul 31. pii: 10.1038/s41586-019-1438-2. doi:, 10.1038/s41586-019-1438-2. PMID:31367042<ref>PMID:31367042</ref>
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==See Also==
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*[[Symporter 3D structures|Symporter 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6npj" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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__TOC__
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[[Category: Brachidanio rerio]]
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[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Feng, L]]
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[[Category: Feng L]]
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[[Category: Liao, M F]]
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[[Category: Liao MF]]
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[[Category: Orlando, B]]
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[[Category: Orlando B]]
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[[Category: Zhang, J R]]
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[[Category: Zhang JR]]
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[[Category: Membrane protein]]
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Current revision

Structure of the NKCC1 CTD

6npj, resolution 3.80Å

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