7lfx: Difference between revisions
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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]] | |||