Structure of the TRPV1 ion channel determined by electron cryo-microscopy

Maofu Liao, Erhu Cao, David Julius () and Yifan Cheng ()
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Maofu Liao: Keck Advanced Microscopy Laboratory, University of California
Erhu Cao: University of California
David Julius: University of California
Yifan Cheng: Keck Advanced Microscopy Laboratory, University of California

Nature, 2013, vol. 504, issue 7478, 107-112

Abstract: 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 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.

Date: 2013
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DOI: 10.1038/nature12822

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