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PDBsum entry 3g3f
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Membrane protein
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PDB id
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3g3f
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Membrane protein
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Title:
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Crystal structure of the glur6 ligand binding domain dimer with glutamate and nacl at 1.38 angstrom resolution
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Structure:
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Glutamate receptor, ionotropic kainate 2. Chain: a, b. Fragment: residues 429-544, 667-806. Synonym: glutamate receptor 6, glur-6, glur6. Engineered: yes
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Source:
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Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: glur6, grik2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.38Å
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R-factor:
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0.153
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R-free:
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0.175
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Authors:
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C.Chaudhry,M.L.Mayer
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Key ref:
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C.Chaudhry
et al.
(2009).
Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
Embo J,
28,
1518-1530.
PubMed id:
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Date:
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02-Feb-09
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Release date:
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02-Jun-09
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PROCHECK
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Headers
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References
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P42260
(GRIK2_RAT) -
Glutamate receptor ionotropic, kainate 2 from Rattus norvegicus
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Seq:
Struc:
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908 a.a.
251 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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Embo J
28:1518-1530
(2009)
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PubMed id:
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Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
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C.Chaudhry,
M.C.Weston,
P.Schuck,
C.Rosenmund,
M.L.Mayer.
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ABSTRACT
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AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor
ligand-binding domains form dimers, which are key functional units controlling
ion-channel activation and desensitization. Dimer stability is inversely related
to the rate and extent of desensitization. Kainate and AMPA receptors share
common structural elements, but functional measurements suggest that subunit
assembly and gating differs between these subtypes. To investigate this, we
constructed a library of GluR6 kainate receptor mutants and directly measured
changes in kainate receptor dimer stability by analytical ultracentrifugation,
which, combined with electrophysiological experiments, revealed an inverse
correlation between dimer stability and the rate of desensitization. We solved
crystal structures for a series of five GluR6 mutants, to understand the
molecular mechanisms for dimer stabilization. We demonstrate that the
desensitized state of kainate receptors acts as a deep energy well offsetting
the stabilizing effects of dimer interface mutants, and that the deactivation of
kainate receptor responses is dominated by entry into desensitized states. Our
results show how neurotransmitter receptors with similar structures and gating
mechanisms can exhibit strikingly different functional properties.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.L.Mayer
(2011).
Glutamate receptor ion channels: where do all the calories go?
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Nat Struct Mol Biol,
18,
253-254.
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M.L.Mayer
(2011).
Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.
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Curr Opin Neurobiol,
21,
283-290.
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R.Ghirlando
(2011).
The analysis of macromolecular interactions by sedimentation equilibrium.
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Methods,
54,
145-156.
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T.Nogi,
N.Yasui,
E.Mihara,
Y.Matsunaga,
M.Noda,
N.Yamashita,
T.Toyofuku,
S.Uchiyama,
Y.Goshima,
A.Kumanogoh,
and
J.Takagi
(2010).
Structural basis for semaphorin signalling through the plexin receptor.
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Nature,
467,
1123-1127.
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PDB codes:
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U.Das,
J.Kumar,
M.L.Mayer,
and
A.J.Plested
(2010).
Domain organization and function in GluK2 subtype kainate receptors.
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Proc Natl Acad Sci U S A,
107,
8463-8468.
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C.Chaudhry,
A.J.Plested,
P.Schuck,
and
M.L.Mayer
(2009).
Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.
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Proc Natl Acad Sci U S A,
106,
12329-12334.
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N.Nayeem,
Y.Zhang,
D.K.Schweppe,
D.R.Madden,
and
T.Green
(2009).
A nondesensitizing kainate receptor point mutant.
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Mol Pharmacol,
76,
534-542.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
