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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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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of the full-length trpv2 channel by cryo-electron microscopy
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Structure:
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Transient receptor potential cation channel subfamily v member 2. Chain: a, b, c, d. Synonym: trpv2, osm-9-like trp channel 2, otrpc2, stretch-activated channel 2b, vanilloid receptor-like protein 1, vrl-1. Engineered: yes
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Source:
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Rattus norvegicus. Organism_taxid: 10116. Expressed in: saccharomycetales. Expression_system_taxid: 4892.
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Authors:
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K.W.Huynh,M.R.Cohen,J.Jiansen,A.Samanta,D.T.Lodowski,Z.H.Zhou, V.Y.Moiseenkova-Bell
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Key ref:
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K.W.Huynh
et al.
(2016).
Structure of the full-length TRPV2 channel by cryo-EM.
Nat Commun,
7,
11130.
PubMed id:
DOI:
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Date:
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11-Jan-16
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Release date:
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30-Mar-16
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PROCHECK
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Headers
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References
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Q9WUD2
(TRPV2_RAT) -
Transient receptor potential cation channel subfamily V member 2 from Rattus norvegicus
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Seq:
Struc:
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761 a.a.
602 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Nat Commun
7:11130
(2016)
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PubMed id:
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Structure of the full-length TRPV2 channel by cryo-EM.
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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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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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Links
