Human mutations highlight an intersubunit cation-&#960; bond that stabilizes the closed but not open or inactivated states of TRPV channels.

Teng, Jinfeng; Anishkin, Andriy; Kung, Ching; Blount, Paul

Human mutations highlight an intersubunit cation-π bond that stabilizes the closed but not open or inactivated states of TRPV channels.

Teng, Jinfeng; Anishkin, Andriy; Kung, Ching; Blount, Paul.

Afiliação

Teng J; Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Anishkin A; Department of Biology, University of Maryland, College Park, MD 20742; anisan@umd.edu ckung@wisc.edu paul.blount@utsouthwestern.edu.
Kung C; Laboratory of Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706; anisan@umd.edu ckung@wisc.edu paul.blount@utsouthwestern.edu.
Blount P; Department of Genetics, University of Wisconsin-Madison, Madison, WI 53706.

Proc Natl Acad Sci U S A ; 116(19): 9410-9416, 2019 05 07.

Article em En | MEDLINE | ID: mdl-31010928

Assuntos

Mutação de Sentido Incorreto; Canais de Cátion TRPV; Substituição de Aminoácidos; Animais; Humanos; Conformação Proteica em alfa-Hélice; Estabilidade Proteica; Saccharomyces cerevisiae/genética; Saccharomyces cerevisiae/metabolismo; Canais de Cátion TRPV/química; Canais de Cátion TRPV/genética; Canais de Cátion TRPV/metabolismo; Xenopus laevis

Palavras-chave

TRP channels; TRP domain; gating; lipids; opening mechanism

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Mutação de Sentido Incorreto / Canais de Cátion TRPV Limite: Animals / Humans Idioma: En Ano de publicação: 2019 Tipo de documento: Article

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