Kevin W Huynh / Matthew R Cohen / Jiansen Jiang / Amrita Samanta / David T Lodowski / Z Hong Zhou / Vera Y Moiseenkova-Bell /
PubMed 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 ...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.
EMDB-6580: Structure of the full-length TRPV2 channel by cryoEM PDB-5hi9: Structure of the full-length TRPV2 channel by cryo-electron microscopy Method: EM (single particle) / Resolution: 4.4 Å
EMDB-6618: Structure of the full-length TRPV2 channel by cryoEM PDB-5hi9: Structure of the full-length TRPV2 channel by cryo-electron microscopy Method: EM (single particle) / Resolution: 4.7 Å
Source
rattus norvegicus (Norway rat)
Keywords
TRANSPORT PROTEIN / TRPV2 ion channel
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Keywords
rattus norvegicus (Norway rat)