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PDBsum entry 4l17
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Transport protein
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PDB id
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4l17
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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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Glua2-l483y-a665c ligand-binding domain in complex with the antagonist dnqx
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Structure:
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Glutamate receptor 2. Chain: a, c, e, g. Fragment: ligand binding domain (unp residues 413-527, 653-796). Synonym: glur-2, ampa-selective glutamate receptor 2, glur-b, glur- k2, glutamate receptor ionotropic, ampa 2, glua2. Engineered: yes. Mutation: yes
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Source:
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Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: gria2, glur2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.80Å
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R-factor:
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0.198
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R-free:
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0.245
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Authors:
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A.Y.Lau,L.Blachowicz,B.Roux
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Key ref:
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A.Y.Lau
et al.
(2013).
A conformational intermediate in glutamate receptor activation.
Neuron,
79,
492-503.
PubMed id:
DOI:
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Date:
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02-Jun-13
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Release date:
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14-Aug-13
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PROCHECK
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Headers
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References
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P19491
(GRIA2_RAT) -
Glutamate receptor 2 from Rattus norvegicus
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Seq:
Struc:
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883 a.a.
259 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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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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DOI no:
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Neuron
79:492-503
(2013)
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PubMed id:
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A conformational intermediate in glutamate receptor activation.
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A.Y.Lau,
H.Salazar,
L.Blachowicz,
V.Ghisi,
A.J.Plested,
B.Roux.
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ABSTRACT
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Ionotropic glutamate receptors (iGluRs) transduce the chemical signal of
neurotransmitter release into membrane depolarization at excitatory synapses in
the brain. The opening of the transmembrane ion channel of these ligand-gated
receptors is driven by conformational transitions that are induced by the
association of glutamate molecules to the ligand-binding domains (LBDs). Here,
we describe the crystal structure of a GluA2 LBD tetramer in a configuration
that involves an ∼30° rotation of the LBD dimers relative to the crystal
structure of the full-length receptor. The configuration is stabilized by an
engineered disulfide crosslink. Biochemical and electrophysiological studies on
full-length receptors incorporating either this crosslink or an engineered metal
bridge show that this LBD configuration corresponds to an intermediate state of
receptor activation. GluA2 activation therefore involves a combination of both
intra-LBD (cleft closure) and inter-LBD dimer conformational transitions.
Overall, these results provide a comprehensive structural characterization of an
iGluR intermediate state.
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Links
