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PDBsum entry 5hi9
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Transport protein
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PDB id
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5hi9
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References listed in PDB file
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Key reference
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Title
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Structure of the full-Length trpv2 channel by cryo-Em.
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Authors
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K.W.Huynh,
M.R.Cohen,
J.Jiang,
A.Samanta,
D.T.Lodowski,
Z.H.Zhou,
V.Y.Moiseenkova-Bell.
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Ref.
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Nat Commun, 2016,
7,
11130.
[DOI no: ]
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PubMed id
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Abstract
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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.
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