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Nat Commun. 2016 Mar 29;7:11130. doi: 10.1038/ncomms11130.

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

Author information

1
Department of Pharmacology, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA.
2
Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, USA.
3
Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, California 90095, USA.
4
California NanoSystems Institute, University of California, Los Angeles, California 90095, USA.
5
Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, USA.

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.

PMID:
27021073
PMCID:
PMC4820614
DOI:
10.1038/ncomms11130
[Indexed for MEDLINE]
Free PMC Article

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