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1.
Nat Struct Mol Biol ; 27(2): 221, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31932763

RESUMO

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

2.
Nat Struct Mol Biol ; 26(11): 994-998, 2019 11.
Artigo em Inglês | MEDLINE | ID: mdl-31636415

RESUMO

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.


Assuntos
Canais de Cátion TRPV/química , Sensação Térmica , Animais , Microscopia Crioeletrônica , Temperatura Alta , Camundongos , Modelos Moleculares , Conformação Proteica , Domínios Proteicos , Canais de Cátion TRPV/metabolismo , Temperatura
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