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TitleTRPV1 structures in distinct conformations reveal activation mechanisms.
Journal, issue, pagesNature, Vol. 504, Issue 7478, Page 113-118, Year 2013
Publish dateDec 5, 2013
AuthorsErhu Cao / Maofu Liao / Yifan Cheng / David Julius /
PubMed AbstractTransient 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 ...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.
External linksNature / PubMed:24305161 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.2 Å
Structure data

5776

3j5q

EMDB-5776: Structure of the capsaicin receptor, TRPV1, in complex with DkTx and RTX determined by single particle electron cryo-microscopy
PDB-3j5q: Structure of TRPV1 ion channel in complex with DkTx and RTX determined by single particle electron cryo-microscopy
Method: EM (single particle) / Resolution: 3.8 Å

5777

3j5r

EMDB-5777: Reconstruction of rat TRPV1 channel in complex with capsaicin by single particle cryo-microscopy
PDB-3j5r: Reconstruction of TRPV1 ion channel in complex with capsaicin by single particle cryo-microscopy
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • rattus norvegicus (Norway rat)
  • chilobrachys guangxiensis (spider)
KeywordsTRANSPORT PROTEIN/TOXIN / TRPV1 channel / DkTx / RTX / TRANSPORT PROTEIN-TOXIN complex / TRANSPORT PROTEIN / capsaicin

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