3a2a: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 3: Line 3:
<StructureSection load='3a2a' size='340' side='right'caption='[[3a2a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3a2a' size='340' side='right'caption='[[3a2a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== 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>
<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 ==
[[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==
==See Also==
Line 25: Line 17:
__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]]
[[Category: Voltage-gated channel]]
[[Category: Voltage-gated proton channel]]

Revision as of 11:40, 7 February 2024

The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

Structural highlights

3a2a is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

3a2a, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3a2a&oldid=4047427"