期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 26, 期 11, 页码 994-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41594-019-0318-7
关键词
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资金
- National Institutes of Health (NIH) [F31 CA232391-01]
- NIH [R01 CA206573, R01 NS083660, R01 NS107253, GM103310]
- National Science Foundation [1818213]
- Irma T. Hirschl Career Scientist Award
- Simons Foundation [349247]
- NYSTAR
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1818213] Funding Source: National Science Foundation
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 alpha-to-pi 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.
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