3a2a

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Revision as of 08:40, 7 February 2024

The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

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@@ Line 3: / Line 3: @@
 <StructureSection load='3a2a' size='340' side='right'caption='[[3a2a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a2a]] is a 4 chain structure with sequence from [https://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 [https://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]] 2&#8491;</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>
 == Function ==
-[[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>
+[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;">
-== 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<ref>PMID:20147290</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3a2a" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[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]]
-[[Category: Voltage-gated channel]]
-[[Category: Voltage-gated proton channel]]

3a2a

From Proteopedia

Revision as of 08:40, 7 February 2024

The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

Structural highlights

Function

See Also

References

Contents

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