西亚试剂：Structure of the TRPV1 ion channel determined by electron c

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

Maofu Liao，Erhu Cao，David Julius& Yifan Cheng

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 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.

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