2mkv

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'''Unreleased structure'''
 
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The entry 2mkv is ON HOLD
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==Structure of the NA,K-ATPASE regulatory protein FXYD2b in micelles==
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<StructureSection load='2mkv' size='340' side='right'caption='[[2mkv]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mkv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MKV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mkv OCA], [https://pdbe.org/2mkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mkv RCSB], [https://www.ebi.ac.uk/pdbsum/2mkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mkv ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ATNG_HUMAN ATNG_HUMAN] Autosomal dominant primary hypomagnesemia with hypocalcuria. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/ATNG_HUMAN ATNG_HUMAN] May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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FXYD2 is a membrane protein responsible for regulating the function of the Na,K-ATPase in mammalian kidney epithelial cells. Here we report the structure of FXYD2b, one of two splice variants of the protein, determined by NMR spectroscopy in detergent micelles. Solid-state NMR characterization of the protein embedded in phospholipid bilayers indicates that several arginine side chains may be involved in hydrogen bond interactions with the phospholipid polar head groups. The structure and the NMR data suggest that FXYD2b could regulate the Na,K-ATPase by modulating the effective membrane surface electrostatics near the ion binding sites of the pump. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.
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Authors: Marassi, F.M., Gong, X.
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Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane-water interfacial arginines.,Gong XM, Ding Y, Yu J, Yao Y, Marassi FM Biochim Biophys Acta. 2014 May 2. pii: S0005-2736(14)00156-4. doi:, 10.1016/j.bbamem.2014.04.021. PMID:24794573<ref>PMID:24794573</ref>
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Description: STRUCTURE OF THE NA,K-ATPASE REGULATORY PROTEIN FXYD2b IN MICELLES
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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 2mkv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Gong X]]
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[[Category: Marassi FM]]

Current revision

Structure of the NA,K-ATPASE regulatory protein FXYD2b in micelles

PDB ID 2mkv

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