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Structure of the full-length TRPV2 channel by cryo-EM.

ABSTRACT: Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ?5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels.

SUBMITTER: Huynh KW

PROVIDER: S-EPMC4820614 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Structure of the full-length TRPV2 channel by cryo-EM.

Huynh Kevin W KW Huynh Kevin W KW Cohen Matthew R MR Jiang Jiansen J Samanta Amrita A Lodowski David T DT Zhou Z Hong ZH Moiseenkova-Bell Vera Y VY

Nature communications 20160329

Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel ...[more]

PMID: 27021073

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