7mxo: Difference between revisions

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-'''Unreleased structure'''
-The entry 7mxo is ON HOLD
+==CryoEM structure of human NKCC1==
+<StructureSection load='7mxo' size='340' side='right'caption='[[7mxo]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7mxo]] 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=7MXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MXO 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]] 3.47&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=7mxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mxo OCA], [https://pdbe.org/7mxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mxo RCSB], [https://www.ebi.ac.uk/pdbsum/7mxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mxo 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 Na-K-2Cl cotransporter-1 (NKCC1) is an electroneutral Na(+)-dependent transporter responsible for simultaneously translocating Na(+), K(+), and Cl(-) ions into cells. In human tissue, NKCC1 plays a critical role in regulating cytoplasmic volume, fluid intake, chloride homeostasis, and cell polarity. Here, we report four structures of human NKCC1 (hNKCC1), both in the absence and presence of loop diuretic (bumetanide or furosemide), using single-particle cryo-electron microscopy. These structures allow us to directly observe various novel conformations of the hNKCC1 dimer. They also reveal two drug-binding sites located at the transmembrane and cytosolic carboxyl-terminal domains, respectively. Together, our findings enable us to delineate an inhibition mechanism that involves a coupled movement between the cytosolic and transmembrane domains of hNKCC1.
-Authors: Moseng, M.A.
+Inhibition mechanism of NKCC1 involves the carboxyl terminus and long-range conformational coupling.,Moseng MA, Su CC, Rios K, Cui M, Lyu M, Glaza P, Klenotic PA, Delpire E, Yu EW Sci Adv. 2022 Oct 28;8(43):eabq0952. doi: 10.1126/sciadv.abq0952. Epub 2022 Oct , 28. PMID:36306358<ref>PMID:36306358</ref>
-Description: Full-length Cryo-EM structure of human NKCC1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Moseng, M.A]]
+<div class="pdbe-citations 7mxo" 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: Moseng MA]]