Maofu Liao / Erhu Cao / David Julius / Yifan Cheng /
PubMed Abstract
Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been ...Transient receptor potential (TRP) channels are sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been hampered by a lack of detailed structural information. Here we exploit advances in electron cryo-microscopy to determine the structure of a mammalian TRP channel, TRPV1, at 3.4 Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Like voltage-gated channels, TRPV1 exhibits four-fold symmetry around a central ion pathway formed by transmembrane segments 5-6 (S5-S6) and the intervening pore loop, which is flanked by S1-S4 voltage-sensor-like domains. TRPV1 has a wide extracellular 'mouth' with a short selectivity filter. The conserved 'TRP domain' interacts with the S4-S5 linker, consistent with its contribution to allosteric modulation. Subunit organization is facilitated by interactions among cytoplasmic domains, including amino-terminal ankyrin repeats. These observations provide a structural blueprint for understanding unique aspects of TRP channel function.
EMDB-5778: Structure of the capsaicin receptor, TRPV1, determined by single particle electron cryo-microscopy PDB-3j5p: Structure of TRPV1 ion channel determined by single particle electron cryo-microscopy Method: EM (single particle) / Resolution: 3.275 Å
Source
rattus norvegicus (Norway rat)
Keywords
TRANSPORT PROTEIN / TRPV1 channel
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TRANSPORT PROTEIN / TRPV1 channel
