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PDBsum entry 4hfh
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Membrane protein, transport protein
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PDB id
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4hfh
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PDB id:
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| Name: |
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Membrane protein, transport protein
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Title:
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The glic pentameric ligand-gated ion channel (wild-type) complexed to bromoform
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Structure:
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Proton-gated ion channel. Chain: a, b, c, d, e. Synonym: glic, ligand-gated ion channel, lgic. Engineered: yes
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Source:
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Gloeobacter violaceus. Organism_taxid: 251221. Strain: pcc 7421. Gene: glvi, glr4197. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.65Å
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R-factor:
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0.203
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R-free:
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0.213
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Authors:
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L.Sauguet,R.J.Howard,L.Malherbe,U.S.Lee,P.J.Corringer,R.A.Harris, M.Delarue
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Key ref:
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L.Sauguet
et al.
(2013).
Structural basis for potentiation by alcohols and anaesthetics in a ligand-gated ion channel.
Nat Commun,
4,
1697.
PubMed id:
DOI:
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Date:
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05-Oct-12
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Release date:
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17-Apr-13
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PROCHECK
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Headers
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References
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Q7NDN8
(GLIC_GLOVI) -
Proton-gated ion channel from Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
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Seq:
Struc:
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359 a.a.
311 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Nat Commun
4:1697
(2013)
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PubMed id:
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Structural basis for potentiation by alcohols and anaesthetics in a ligand-gated ion channel.
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L.Sauguet,
R.J.Howard,
L.Malherbe,
U.S.Lee,
P.J.Corringer,
R.A.Harris,
M.Delarue.
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ABSTRACT
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Ethanol alters nerve signalling by interacting with proteins in the central
nervous system, particularly pentameric ligand-gated ion channels. A recent
series of mutagenesis experiments on Gloeobacter violaceus ligand-gated ion
channel, a prokaryotic member of this family, identified a single-site variant
that is potentiated by pharmacologically relevant concentrations of ethanol.
Here we determine crystal structures of the ethanol-sensitized variant in the
absence and presence of ethanol and related modulators, which bind in a
transmembrane cavity between channel subunits and may stabilize the open form of
the channel. Structural and mutagenesis studies defined overlapping mechanisms
of potentiation by alcohols and anaesthetics via the inter-subunit cavity.
Furthermore, homology modelling show this cavity to be conserved in human
ethanol-sensitive glycine and GABA(A) receptors, and to involve residues
previously shown to influence alcohol and anaesthetic action on these proteins.
These results suggest a common structural basis for ethanol potentiation of an
important class of targets for neurological actions of ethanol.
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