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| | <StructureSection load='3a2a' size='340' side='right'caption='[[3a2a]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3a2a' size='340' side='right'caption='[[3a2a]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a2a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A2A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A2A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A2A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2a OCA], [http://pdbe.org/3a2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a2a RCSB], [http://www.ebi.ac.uk/pdbsum/3a2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2a ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3a2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a2a OCA], [https://pdbe.org/3a2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a2a RCSB], [https://www.ebi.ac.uk/pdbsum/3a2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a2a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HVCN1_HUMAN HVCN1_HUMAN]] 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.<ref>PMID:16554753</ref> <ref>PMID:20037153</ref> <ref>PMID:22020278</ref> | + | [https://www.uniprot.org/uniprot/HVCN1_HUMAN HVCN1_HUMAN] 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.<ref>PMID:16554753</ref> <ref>PMID:20037153</ref> <ref>PMID:22020278</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, S J]] | + | [[Category: Li SJ]] |
| - | [[Category: Sun, F]] | + | [[Category: Sun F]] |
| - | [[Category: Unno, H]] | + | [[Category: Unno H]] |
| - | [[Category: Zhai, Y]] | + | [[Category: Zhai Y]] |
| - | [[Category: Zhao, Q]] | + | [[Category: Zhao Q]] |
| - | [[Category: Zhou, Q]] | + | [[Category: Zhou Q]] |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Ionic channel]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
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| - | [[Category: Voltage-gated channel]]
| + | |
| - | [[Category: Voltage-gated proton channel]]
| + | |
| Structural highlights
Function
HVCN1_HUMAN 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.[1] [2] [3]
Publication Abstract from PubMed
The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.
The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.,Li SJ, Zhao Q, Zhou Q, Unno H, Zhai Y, Sun F J Biol Chem. 2010 Apr 16;285(16):12047-54. Epub 2010 Feb 10. PMID:20147290[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramsey IS, Moran MM, Chong JA, Clapham DE. A voltage-gated proton-selective channel lacking the pore domain. Nature. 2006 Apr 27;440(7088):1213-6. Epub 2006 Mar 22. PMID:16554753 doi:http://dx.doi.org/nature04700
- ↑ Musset B, Capasso M, Cherny VV, Morgan D, Bhamrah M, Dyer MJ, DeCoursey TE. Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes. J Biol Chem. 2010 Feb 19;285(8):5117-21. doi: 10.1074/jbc.C109.082727. Epub 2009 , Dec 26. PMID:20037153 doi:http://dx.doi.org/10.1074/jbc.C109.082727
- ↑ Musset B, Smith SM, Rajan S, Morgan D, Cherny VV, Decoursey TE. Aspartate 112 is the selectivity filter of the human voltage-gated proton channel. Nature. 2011 Oct 23;480(7376):273-7. doi: 10.1038/nature10557. PMID:22020278 doi:http://dx.doi.org/10.1038/nature10557
- ↑ Li SJ, Zhao Q, Zhou Q, Unno H, Zhai Y, Sun F. The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1. J Biol Chem. 2010 Apr 16;285(16):12047-54. Epub 2010 Feb 10. PMID:20147290 doi:10.1074/jbc.M109.040360
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