5oqk - Revision history

OCA at 10:24, 14 June 2023

OCA — Wed, 14 Jun 2023 10:24:13 GMT

←Older revision		Revision as of 10:24, 14 June 2023
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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 ==
Line 25:		Line 24:
	__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~~]]	+

OCA at 11:24, 13 November 2019

OCA — Wed, 13 Nov 2019 11:24:06 GMT

←Older revision		Revision as of 11:24, 13 November 2019
Line 9:		Line 9:
	== 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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== 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<ref>PMID:31365236</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5oqk" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:20, 6 November 2019

OCA — Wed, 06 Nov 2019 07:20:32 GMT

←Older revision		Revision as of 07:20, 6 November 2019
Line 3:		Line 3:
	<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]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5oqk]] is a 1 chain structure. 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 [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>
-	</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>	+	</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>
		+	<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>		[[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>
		+
		+	==See Also==
		+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Bayrhuber, M]]		[[Category: Bayrhuber, M]]

OCA at 06:47, 3 April 2019

OCA — Wed, 03 Apr 2019 06:47:25 GMT

←Older revision		Revision as of 06:47, 3 April 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5oqk ~~is ON HOLD~~	+	==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=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5oqk]] is a 1 chain structure. 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>
-	~~Description~~:	+	</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>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	== 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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bayrhuber, M]]
		+	[[Category: Eichmann, C]]
		+	[[Category: Kwiatowski, W]]
		+	[[Category: Maslennikov, I]]
		+	[[Category: Riek, R]]
		+	[[Category: Sobol, A]]
		+	[[Category: Wierschem, C]]
		+	[[Category: Anti-parallel four-helix bundle]]
		+	[[Category: Membrane protein]]
		+	[[Category: Proton transport]]
		+	[[Category: Voltage gated proton channel]]

OCA: Protected "5oqk" [edit=sysop:move=sysop]

OCA — Wed, 27 Sep 2017 12:43:33 GMT

Protected "5oqk" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:43, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5oqk is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 27 Sep 2017 12:43:32 GMT

New page: '''Unreleased structure''' The entry 5oqk is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5oqk is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]