TRPV1 structures in distinct conformations reveal activation mechanisms View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-12

AUTHORS

Erhu Cao, Maofu Liao, Yifan Cheng, David Julius

ABSTRACT

Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor, TRPV1. A domain (consisting of transmembrane segments 1-4) that moves during activation of voltage-gated channels remains stationary in TRPV1, highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a hydrophobic constriction at the lower gate, suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels. More... »

PAGES

113

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature12823

DOI

http://dx.doi.org/10.1038/nature12823

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036688363

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24305161


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303 schema:name Department of Physiology, University of California, San Francisco, California 94158-2517, USA
304 Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158-2517, USA
305 rdf:type schema:Organization
 




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