6c8h: Difference between revisions
New page: '''Unreleased structure''' The entry 6c8h is ON HOLD Authors: Deng, Z., Paknejad, N., Maksaev, G., Sala-Rabanal, M., Nichols, C.G., Hite, R.K., Yuan, P. Description: Crystal structure ... |
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==Crystal structure of Transient Receptor Potential (TRP) channel TRPV4 in the presence of gadolinium== | |||
<StructureSection load='6c8h' size='340' side='right'caption='[[6c8h]], [[Resolution|resolution]] 6.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6c8h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C8H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</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=6c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c8h OCA], [https://pdbe.org/6c8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c8h RCSB], [https://www.ebi.ac.uk/pdbsum/6c8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c8h ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The transient receptor potential (TRP) channel TRPV4 participates in multiple biological processes, and numerous TRPV4 mutations underlie several distinct and devastating diseases. Here we present the cryo-EM structure of Xenopus tropicalis TRPV4 at 3.8-A resolution. The ion-conduction pore contains an intracellular gate formed by the inner helices, but lacks any extracellular gate in the selectivity filter, as observed in other TRPV channels. Anomalous X-ray diffraction analyses identify a single ion-binding site in the selectivity filter, thus explaining TRPV4 nonselectivity. Structural comparisons with other TRP channels and distantly related voltage-gated cation channels reveal an unprecedented, unique packing interface between the voltage-sensor-like domain and the pore domain, suggesting distinct gating mechanisms. Moreover, our structure begins to provide mechanistic insights to the large set of pathogenic mutations, offering potential opportunities for drug development. | |||
Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.,Deng Z, Paknejad N, Maksaev G, Sala-Rabanal M, Nichols CG, Hite RK, Yuan P Nat Struct Mol Biol. 2018 Mar;25(3):252-260. doi: 10.1038/s41594-018-0037-5. Epub, 2018 Feb 26. PMID:29483651<ref>PMID:29483651</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6c8h" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Nichols | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Xenopus tropicalis]] | |||
[[Category: Deng Z]] | |||
[[Category: Hite RK]] | |||
[[Category: Maksaev G]] | |||
[[Category: Nichols CG]] | |||
[[Category: Paknejad N]] | |||
[[Category: Sala-Rabanal M]] | |||
[[Category: Yuan P]] | |||
Latest revision as of 17:58, 4 October 2023
Crystal structure of Transient Receptor Potential (TRP) channel TRPV4 in the presence of gadoliniumCrystal structure of Transient Receptor Potential (TRP) channel TRPV4 in the presence of gadolinium
Structural highlights
Publication Abstract from PubMedThe transient receptor potential (TRP) channel TRPV4 participates in multiple biological processes, and numerous TRPV4 mutations underlie several distinct and devastating diseases. Here we present the cryo-EM structure of Xenopus tropicalis TRPV4 at 3.8-A resolution. The ion-conduction pore contains an intracellular gate formed by the inner helices, but lacks any extracellular gate in the selectivity filter, as observed in other TRPV channels. Anomalous X-ray diffraction analyses identify a single ion-binding site in the selectivity filter, thus explaining TRPV4 nonselectivity. Structural comparisons with other TRP channels and distantly related voltage-gated cation channels reveal an unprecedented, unique packing interface between the voltage-sensor-like domain and the pore domain, suggesting distinct gating mechanisms. Moreover, our structure begins to provide mechanistic insights to the large set of pathogenic mutations, offering potential opportunities for drug development. Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms.,Deng Z, Paknejad N, Maksaev G, Sala-Rabanal M, Nichols CG, Hite RK, Yuan P Nat Struct Mol Biol. 2018 Mar;25(3):252-260. doi: 10.1038/s41594-018-0037-5. Epub, 2018 Feb 26. PMID:29483651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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