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| | ==Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)== | | ==Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)== |
| - | <StructureSection load='5oqk' size='340' side='right'caption='[[5oqk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5oqk' size='340' side='right'caption='[[5oqk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oqk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OQK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oqk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OQK FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HVCN1, VSOP, UNQ578/PRO1140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5oqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqk OCA], [https://pdbe.org/5oqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oqk RCSB], [https://www.ebi.ac.uk/pdbsum/5oqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqk 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=5oqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqk OCA], [http://pdbe.org/5oqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oqk RCSB], [http://www.ebi.ac.uk/pdbsum/5oqk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqk 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: Bayrhuber, M]] | + | [[Category: Bayrhuber M]] |
| - | [[Category: Eichmann, C]] | + | [[Category: Eichmann C]] |
| - | [[Category: Kwiatowski, W]] | + | [[Category: Kwiatowski W]] |
| - | [[Category: Maslennikov, I]] | + | [[Category: Maslennikov I]] |
| - | [[Category: Riek, R]] | + | [[Category: Riek R]] |
| - | [[Category: Sobol, A]] | + | [[Category: Sobol A]] |
| - | [[Category: Wierschem, C]] | + | [[Category: Wierschem C]] |
| - | [[Category: Anti-parallel four-helix bundle]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Proton transport]]
| + | |
| - | [[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 human voltage-gated proton channel [Hv1((1)) or VSDO((2))] plays an important role in the human innate immune system. Its structure differs considerably from those of other cation channels. It is built solely of a voltage-sensing domain and thus lacks the central pore domain, which is essential for other cation channels. Here, we determined the solution structure of an N- and C-terminally truncated human Hv1 (Delta-Hv1) in the resting state by nuclear magnetic resonance (NMR) spectroscopy. Delta-Hv1 comprises the typical voltage-sensing antiparallel four-helix bundle (S1-S4) preceded by an amphipathic helix (S0). The solution structure corresponds to an intermediate state between resting and activated forms of voltage-sensing domains. Furthermore, Zn(2+)-induced closing of proton channel Delta-Hv1 was studied with two-dimensional NMR spectroscopy, which showed that characteristic large scale dynamics of open Delta-Hv1 are absent in the closed state of the channel. Additionally, pH titration studies demonstrated that a higher H(+) concentration is required for the protonation of side chains in the Zn(2+)-induced closed state than in the open state. These observations demonstrate both structural and dynamical changes involved in the process of voltage gating of the Hv1 channel and, in the future, may help to explain the unique properties of unidirectional conductance and the exceptional ion selectivity of the channel.
Nuclear Magnetic Resonance Solution Structure and Functional Behavior of the Human Proton Channel.,Bayrhuber M, Maslennikov I, Kwiatkowski W, Sobol A, Wierschem C, Eichmann C, Frey L, Riek R Biochemistry. 2019 Oct 1;58(39):4017-4027. doi: 10.1021/acs.biochem.9b00471. Epub, 2019 Sep 21. PMID:31365236[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
- ↑ Bayrhuber M, Maslennikov I, Kwiatkowski W, Sobol A, Wierschem C, Eichmann C, Frey L, Riek R. Nuclear Magnetic Resonance Solution Structure and Functional Behavior of the Human Proton Channel. Biochemistry. 2019 Oct 1;58(39):4017-4027. doi: 10.1021/acs.biochem.9b00471. Epub, 2019 Sep 21. PMID:31365236 doi:http://dx.doi.org/10.1021/acs.biochem.9b00471
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