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6v1q
From Proteopedia
(Difference between revisions)
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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=6v1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1q OCA], [http://pdbe.org/6v1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v1q RCSB], [http://www.ebi.ac.uk/pdbsum/6v1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1q ProSAT]</span></td></tr> | <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=6v1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v1q OCA], [http://pdbe.org/6v1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v1q RCSB], [http://www.ebi.ac.uk/pdbsum/6v1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v1q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Voltage-gated ion channels endow membranes with excitability and the means to propagate action potentials that form the basis of all neuronal signaling. We determined the structure of a voltage-gated sodium channel, two-pore channel 3 (TPC3), which generates ultralong action potentials. TPC3 is distinguished by activation only at extreme membrane depolarization (V50 approximately +75 mV), in contrast to other TPCs and NaV channels that activate between -20 and 0 mV. We present electrophysiological evidence that TPC3 voltage activation depends only on voltage sensing domain 2 (VSD2) and that each of the three gating arginines in VSD2 reduces the activation threshold. The structure presents a chemical basis for sodium selectivity, and a constricted gate suggests a closed pore consistent with extreme voltage dependence. The structure, confirmed by our electrophysiology, illustrates the configuration of a bona fide resting state voltage sensor, observed without the need for any inhibitory ligand, and independent of any chemical or mutagenic alteration. | ||
| + | |||
| + | Resting state structure of the hyperdepolarization activated two-pore channel 3.,Dickinson MS, Myasnikov A, Eriksen J, Poweleit N, Stroud RM Proc Natl Acad Sci U S A. 2020 Jan 10. pii: 1915144117. doi:, 10.1073/pnas.1915144117. PMID:31924746<ref>PMID:31924746</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6v1q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:00, 22 January 2020
Two-pore channel 3
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