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6npk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the TM domain== | |
| + | <SX load='6npk' size='340' side='right' viewer='molstar' caption='[[6npk]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6npk]] 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=6NPK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6NPK FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6npk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6npk OCA], [http://pdbe.org/6npk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6npk RCSB], [http://www.ebi.ac.uk/pdbsum/6npk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6npk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6npk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Brachidanio rerio]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Feng, L]] | ||
| + | [[Category: Liao, M F]] | ||
| + | [[Category: Orlando, B]] | ||
| + | [[Category: Zhang, J R]] | ||
| + | [[Category: Membrane protein]] | ||
Current revision
Structure of the TM domain
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