Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms11130
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Funding
- National Institutes of Health Core Grant [EY11373]
- NIH [1S10RR23057, 1S10OD018111]
- NSF [DBI-1338135]
- CNSI at UCLA
- American Heart Association (NCRP Scientist Development Grant) [11SDG5280029]
- National Institute of Health [R01GM103899, R00EY019718]
- Direct For Biological Sciences [1338135] Funding Source: National Science Foundation
- Div Of Biological Infrastructure [1338135] Funding Source: National Science Foundation
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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 similar to 5 angstrom 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.
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