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Nat Struct Mol Biol 2018 Mar 01;253:252-260. doi: 10.1038/s41594-018-0037-5.
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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 .

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-Å 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.

PubMed ID: 29483651
PMC ID: PMC6252174
Article link: Nat Struct Mol Biol
Grant support: [+]

Species referenced: Xenopus tropicalis
Genes referenced: trpv4
GO keywords: voltage-gated cation channel activity [+]

References [+] :
Adams, PHENIX: a comprehensive Python-based system for macromolecular structure solution. 2010, Pubmed