3vmx
From Proteopedia
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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=3vmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmx RCSB], [http://www.ebi.ac.uk/pdbsum/3vmx PDBsum]</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=3vmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmx RCSB], [http://www.ebi.ac.uk/pdbsum/3vmx PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HVCN1_MOUSE HVCN1_MOUSE]] Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 12:02, 25 December 2014
Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel
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