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

Kevin W. Huynh, Matthew R. Cohen, Jiansen Jiang, Amrita Samanta, David T. Lodowski, Z. Hong Zhou and Vera Y. Moiseenkova-Bell ()
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Kevin W. Huynh: School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
Matthew R. Cohen: School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
Jiansen Jiang: Immunology and Molecular Genetics, University of California
Amrita Samanta: School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
David T. Lodowski: School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
Z. Hong Zhou: Immunology and Molecular Genetics, University of California
Vera Y. Moiseenkova-Bell: School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA

Nature Communications, 2016, vol. 7, issue 1, 1-8

Abstract: Abstract Transient receptor potential (TRP) proteins form a superfamily Ca2+-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.

Date: 2016
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DOI: 10.1038/ncomms11130

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