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Structural basis of TRPV1 modulation by endogenous bioactive lipids - Nature Structural & Molecular Biology

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Structural basis of TRPV1 modulation by endogenous bioactive lipids - Nature Structural & Molecular Biology

TRP ion channels are modulated by phosphoinositide lipids, but the underlying structural mechanisms remain unclear. The capsaicin- and heat-activated receptor, TRPV1, has served as a model for deciphering lipid modulation, which is relevant to understanding how pro-algesic agents enhance channel activity in the setting of inflammatory pain. Identification of a pocket within the TRPV1 transmembrane core has provided initial clues as to how phosphoinositide lipids bind to and regulate the channel.

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Structural basis of TRPV1 modulation by endogenous bioactive lipids - Nature Structural & Molecular Biology

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Structural basis of TRPV1 modulation by endogenous bioactive lipids - Nature Structural & Molecular Biology

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