3vmy

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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=3vmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmy RCSB], [http://www.ebi.ac.uk/pdbsum/3vmy 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=3vmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vmy RCSB], [http://www.ebi.ac.uk/pdbsum/3vmy PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[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).
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</StructureSection>
</StructureSection>

Revision as of 22:25, 24 December 2014

Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel (REDUCTION/DTT)

3vmy, resolution 1.47Å

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