7lfx - Revision history

OCA at 14:59, 6 March 2024

2024-03-06T14:59:16Z

←Older revision		Revision as of 14:59, 6 March 2024
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	<StructureSection load='7lfx' size='340' side='right'caption='[[7lfx]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='7lfx' size='340' side='right'caption='[[7lfx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7lfx]] 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=7LFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LFX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7lfx]] 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=7LFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LFX FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.1Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CNGA1, CNCG, CNCG1 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</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=7lfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lfx OCA], [https://pdbe.org/7lfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lfx RCSB], [https://www.ebi.ac.uk/pdbsum/7lfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lfx 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=7lfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lfx OCA], [https://pdbe.org/7lfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lfx RCSB], [https://www.ebi.ac.uk/pdbsum/7lfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lfx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN]] Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN] Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN]] Subunit of the rod cyclic GMP-gated cation channel, which is involved in the final stage of the phototransduction pathway. When light hits rod photoreceptors, cGMP concentrations decrease causing rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization of the membrane potential.[UniProtKB:Q00194]	+	[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN] Subunit of the rod cyclic GMP-gated cation channel, which is involved in the final stage of the phototransduction pathway. When light hits rod photoreceptors, cGMP concentrations decrease causing rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization of the membrane potential.[UniProtKB:Q00194]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structural analyses of ion binding profiles in the selectivity filters of the wild-type channel and the E365Q filter mutant allow us to unambiguously define the two Ca(2+) binding sites inside the selectivity filter, providing structural insights into Ca(2+) blockage and permeation in CNG channels. The structure of the E365Q mutant also reveals two alternative side-chain conformations at Q365, providing a plausible explanation for the voltage-dependent gating of CNG channel acquired upon E365 mutation.	+

-	Structural mechanisms of gating and selectivity of human rod CNGA1 channel.,Xue J, Han Y, Zeng W, Wang Y, Jiang Y Neuron. 2021 Feb 19. pii: S0896-6273(21)00081-7. doi:, 10.1016/j.neuron.2021.02.007. PMID:33651975<ref>PMID:33651975</ref>	+	==See Also==
-		+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7lfx" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Han, Y]]	+	[[Category: Han Y]]
-	[[Category: Jiang, Y]]	+	[[Category: Jiang Y]]
-	[[Category: Xue, J]]	+	[[Category: Xue J]]
-	~~[[Category: Alpha-helical]]~~	+
-	~~[[Category: Ion channel]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 09:14, 5 May 2021

2021-05-05T09:14:19Z

←Older revision		Revision as of 09:14, 5 May 2021
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	==Cryo-EM structure of human cGMP-bound open CNGA1 channel in Na+/Ca2+==		==Cryo-EM structure of human cGMP-bound open CNGA1 channel in Na+/Ca2+==
-	<StructureSection load='7lfx' size='340' side='right'caption='[[7lfx]]' scene=''>	+	<StructureSection load='7lfx' size='340' side='right'caption='[[7lfx]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LFX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7lfx]] 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=7LFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LFX FirstGlance]. <br>
-	</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=7lfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lfx OCA], [https://pdbe.org/7lfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lfx RCSB], [https://www.ebi.ac.uk/pdbsum/7lfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lfx ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CNGA1, CNCG, CNCG1 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7lfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lfx OCA], [https://pdbe.org/7lfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lfx RCSB], [https://www.ebi.ac.uk/pdbsum/7lfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lfx ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN]] Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry.
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/CNGA1_HUMAN CNGA1_HUMAN]] Subunit of the rod cyclic GMP-gated cation channel, which is involved in the final stage of the phototransduction pathway. When light hits rod photoreceptors, cGMP concentrations decrease causing rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization of the membrane potential.[UniProtKB:Q00194]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structural analyses of ion binding profiles in the selectivity filters of the wild-type channel and the E365Q filter mutant allow us to unambiguously define the two Ca(2+) binding sites inside the selectivity filter, providing structural insights into Ca(2+) blockage and permeation in CNG channels. The structure of the E365Q mutant also reveals two alternative side-chain conformations at Q365, providing a plausible explanation for the voltage-dependent gating of CNG channel acquired upon E365 mutation.
		+
		+	Structural mechanisms of gating and selectivity of human rod CNGA1 channel.,Xue J, Han Y, Zeng W, Wang Y, Jiang Y Neuron. 2021 Feb 19. pii: S0896-6273(21)00081-7. doi:, 10.1016/j.neuron.2021.02.007. PMID:33651975<ref>PMID:33651975</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7lfx" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Han Y]]	+	[[Category: Han, Y]]
-	[[Category: Jiang Y]]	+	[[Category: Jiang, Y]]
-	[[Category: Xue J]]	+	[[Category: Xue, J]]
		+	[[Category: Alpha-helical]]
		+	[[Category: Ion channel]]
		+	[[Category: Membrane protein]]

OCA at 17:24, 10 March 2021

2021-03-10T17:24:08Z

←Older revision		Revision as of 17:24, 10 March 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7lfx is ~~ON HOLD until Paper Publication~~	+	==Cryo-EM structure of human cGMP-bound open CNGA1 channel in Na+/Ca2+==
-		+	<StructureSection load='7lfx' size='340' side='right'caption='[[7lfx]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LFX FirstGlance]. <br>
-	~~Description~~:	+	</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=7lfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lfx OCA], [https://pdbe.org/7lfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lfx RCSB], [https://www.ebi.ac.uk/pdbsum/7lfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lfx ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Han Y]]
		+	[[Category: Jiang Y]]
		+	[[Category: Xue J]]

OCA at 09:27, 3 February 2021

2021-02-03T09:27:30Z

←Older revision		Revision as of 09:27, 3 February 2021
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7lfx is ON HOLD	+	The entry 7lfx is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7lfx" [edit=sysop:move=sysop]

2021-01-27T06:48:24Z

Protected "7lfx" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:48, 27 January 2021

OCA: New page: '''Unreleased structure''' The entry 7lfx is ON HOLD Authors: Description: Category: Unreleased Structures

2021-01-27T06:48:23Z

New page: '''Unreleased structure''' The entry 7lfx is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7lfx is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]