Structural snapshots of TRPV1 reveal mechanism of polymodal functionality

• Published in: Cell Vol. 184; no. 20; pp. 5138 - 5150.e12
• Main Authors: Zhang, Kaihua, Julius, David, Cheng, Yifan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.09.2021
• Subjects: Allosteric Regulation; Cell Membrane Permeability - drug effects; cryo-electron microscopy; cryo-EM structure; Cryoelectron Microscopy; Diterpenes - pharmacology; HEK293 Cells; Humans; ion channel; Ion Channel Gating; ion pore permeability; ligands; Lipids - chemistry; Meglumine - pharmacology; Models, Molecular; peptides; permeability; plasticity; Protein Binding; Protein Conformation; Protons; transient receptor potential vanilloid channels; TRP channel; TRP channel gating; TRP channel polymodality; TRPV Cation Channels - agonists; TRPV Cation Channels - chemistry; TRPV Cation Channels - metabolism; TRPV1; TRP channel gating; TRP channel polymodality; TRP channel; ion channel; cryo-EM structure; TRPV1; ion pore permeability

Many transient receptor potential (TRP) channels respond to diverse stimuli and conditionally conduct small and large cations. Such functional plasticity is presumably enabled by a uniquely dynamic ion selectivity filter that is regulated by physiological agents. What is currently missing is a “phot...