6bbj
From Proteopedia
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<SX load='6bbj' size='340' side='right' viewer='molstar' caption='[[6bbj]], [[Resolution|resolution]] 3.80Å' scene=''> | <SX load='6bbj' size='340' side='right' viewer='molstar' caption='[[6bbj]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6bbj]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6bbj]] is a 4 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=6BBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BBJ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6bbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbj OCA], [https://pdbe.org/6bbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bbj RCSB], [https://www.ebi.ac.uk/pdbsum/6bbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbj ProSAT]</span></td></tr> |
</table> | </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. | ||
- | + | ==See Also== | |
- | + | *[[Ion channels 3D structures|Ion channels 3D structures]] | |
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__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Xenopus tropicalis]] |
- | [[Category: | + | [[Category: Deng Z]] |
- | [[Category: | + | [[Category: Hite RK]] |
- | [[Category: | + | [[Category: Yuan P]] |
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Current revision
Xenopus Tropicalis TRPV4
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