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| ==Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel== | | ==Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel== |
| <StructureSection load='3vmx' size='340' side='right' caption='[[3vmx]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='3vmx' size='340' side='right'caption='[[3vmx]], [[Resolution|resolution]] 1.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3vmx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VMX FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3vmx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VMX FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vmy|3vmy]], [[3vmz|3vmz]], [[3vn0|3vn0]]</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]] 1.45Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bts, Hvcn1, Vsop ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3vmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vmx OCA], [https://pdbe.org/3vmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vmx RCSB], [https://www.ebi.ac.uk/pdbsum/3vmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vmx 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=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 == | | == 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). | | [https://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;">
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| == Publication Abstract from PubMed ==
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| Hv1/VSOP is a dimeric voltage-gated H(+) channel in which the gating of one subunit is reportedly coupled to that of the other subunit within the dimer. The molecular basis for dimer formation and intersubunit coupling, however, remains unknown. Here we show that the carboxy terminus ends downstream of the S4 voltage-sensor helix twist in a dimer coiled-coil architecture, which mediates cooperative gating. We also show that the temperature-dependent activation of H(+) current through Hv1/VSOP is regulated by thermostability of the coiled-coil domain, and that this regulation is altered by mutation of the linker between S4 and the coiled-coil. Cooperative gating within the dimer is also dependent on the linker structure, which circular dichroism spectrum analysis suggests is alpha-helical. Our results indicate that the cytoplasmic coiled-coil strands form continuous alpha-helices with S4 and mediate cooperative gating to adjust the range of temperatures over which Hv1/VSOP operates.
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| The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H(+) channel Hv1.,Fujiwara Y, Kurokawa T, Takeshita K, Kobayashi M, Okochi Y, Nakagawa A, Okamura Y Nat Commun. 2012 May 8;3:816. doi: 10.1038/ncomms1823. PMID:22569364<ref>PMID:22569364</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Ion channels|Ion channels]] | | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| [[Category: Fujiwara, Y]] | | [[Category: Fujiwara Y]] |
| [[Category: Kobayashi, M]] | | [[Category: Kobayashi M]] |
| [[Category: Nakagawa, A]] | | [[Category: Nakagawa A]] |
| [[Category: Okamura, Y]] | | [[Category: Okamura Y]] |
| [[Category: Takeshita, K]] | | [[Category: Takeshita K]] |
| [[Category: Coiled-coil]]
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| [[Category: Ion channel]]
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| [[Category: Ion transport]]
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| [[Category: Membrane protein]]
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