Structural basis of temperature sensation by the TRP channel TRPV3
Copyright policy )Structural basis of temperature sensation by the TRP channel TRPV3
We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains.
- University of Illinois at Urbana Champaign United States
- Carnegie Mellon University United States
- COLUMBIA UNIVERSITY HEALTH SCIENCES
- Department of Biochemistry and Molecular Biophysics Columbia University United States
- King’s University United States
Models, Molecular, Hot Temperature, Protein Conformation, Cryoelectron Microscopy, Temperature, TRPV Cation Channels, Article, Mice, Protein Domains, Animals, Thermosensing
Models, Molecular, Hot Temperature, Protein Conformation, Cryoelectron Microscopy, Temperature, TRPV Cation Channels, Article, Mice, Protein Domains, Animals, Thermosensing
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