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7p1i
From Proteopedia
(Difference between revisions)
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</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=7p1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p1i OCA], [https://pdbe.org/7p1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p1i RCSB], [https://www.ebi.ac.uk/pdbsum/7p1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p1i ProSAT]</span></td></tr> | </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=7p1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p1i OCA], [https://pdbe.org/7p1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p1i RCSB], [https://www.ebi.ac.uk/pdbsum/7p1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p1i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Na(+)/H(+) exchanger SLC9B2, also known as NHA2, correlates with the long-sought-after Na(+)/Li(+) exchanger linked to the pathogenesis of diabetes mellitus and essential hypertension in humans. Despite the functional importance of NHA2, structural information and the molecular basis for its ion-exchange mechanism have been lacking. Here we report the cryo-EM structures of bison NHA2 in detergent and in nanodiscs, at 3.0 and 3.5 A resolution, respectively. The bison NHA2 structure, together with solid-state membrane-based electrophysiology, establishes the molecular basis for electroneutral ion exchange. NHA2 consists of 14 transmembrane (TM) segments, rather than the 13 TMs previously observed in mammalian Na(+)/H(+) exchangers (NHEs) and related bacterial antiporters. The additional N-terminal helix in NHA2 forms a unique homodimer interface with a large intracellular gap between the protomers, which closes in the presence of phosphoinositol lipids. We propose that the additional N-terminal helix has evolved as a lipid-mediated remodeling switch for the regulation of NHA2 activity. | ||
| + | |||
| + | Structure, mechanism and lipid-mediated remodeling of the mammalian Na(+)/H(+) exchanger NHA2.,Matsuoka R, Fudim R, Jung S, Zhang C, Bazzone A, Chatzikyriakidou Y, Robinson CV, Nomura N, Iwata S, Landreh M, Orellana L, Beckstein O, Drew D Nat Struct Mol Biol. 2022 Feb;29(2):108-120. doi: 10.1038/s41594-022-00738-2., Epub 2022 Feb 16. PMID:35173351<ref>PMID:35173351</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7p1i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:30, 2 March 2022
Cryo EM structure of bison NHA2 in detergent and N-terminal extension helix
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