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Structural basis of temperature sensation by the TRP channel TRPV3.
Singh AK, McGoldrick LL, Demirkhanyan L, Leslie M, Zakharian E, Sobolevsky AI. Singh AK, et al. Nat Struct Mol Biol. 2019 Nov;26(11):994-998. doi: 10.1038/s41594-019-0318-7. Epub 2019 Oct 21. Nat Struct Mol Biol. 2019. PMID: 31636415 Free PMC article.
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 re …
We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-ste …
TRPV3 is a calcium-permeable temperature-sensitive cation channel.
Xu H, Ramsey IS, Kotecha SA, Moran MM, Chong JA, Lawson D, Ge P, Lilly J, Silos-Santiago I, Xie Y, DiStefano PS, Curtis R, Clapham DE. Xu H, et al. Nature. 2002 Jul 11;418(6894):181-6. doi: 10.1038/nature00882. Epub 2002 Jun 23. Nature. 2002. PMID: 12077604
Transient receptor potential (TRP) proteins are cation-selective channels that function in processes as diverse as sensation and vasoregulation. Mammalian TRP channels that are gated by heat and capsaicin (>43 degrees C; TRPV1 (ref. 1)), noxi …
Transient receptor potential (TRP) proteins are cation-selective channels that function in processes as diverse as sensatio