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Cryo-electron microscopy structure of the TRPV2 ion channel.
Zubcevic, Lejla; Herzik, Mark A; Chung, Ben C; Liu, Zhirui; Lander, Gabriel C; Lee, Seok-Yong.
Afiliación
  • Zubcevic L; Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
  • Herzik MA; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
  • Chung BC; Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
  • Liu Z; Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
  • Lander GC; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
  • Lee SY; Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
Nat Struct Mol Biol ; 23(2): 180-186, 2016 Feb.
Article en En | MEDLINE | ID: mdl-26779611
Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales Catiónicos TRPV Límite: Animals Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales Catiónicos TRPV Límite: Animals Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos