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PDBsum entry 2qs1
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Membrane protein
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PDB id
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2qs1
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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 glur5 ligand binding core dimer in complex with ubp315 at 1.80 angstroms resolution
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Structure:
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Glutamate receptor, ionotropic kainate 1. Chain: a, b. Synonym: glutamate receptor 5, glur-5, glur5. Engineered: yes. Mutation: yes
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: grik1, glur5. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.80Å
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R-factor:
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0.199
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R-free:
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0.219
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Authors:
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G.M.Alushin,D.E.Jane,M.L.Mayer
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Key ref:
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G.M.Alushin
et al.
(2011).
Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists.
Neuropharmacology,
60,
126-134.
PubMed id:
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Date:
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30-Jul-07
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Release date:
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05-Aug-08
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PROCHECK
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Headers
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References
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P22756
(GRIK1_RAT) -
Glutamate receptor ionotropic, kainate 1 from Rattus norvegicus
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Seq:
Struc:
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949 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Neuropharmacology
60:126-134
(2011)
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PubMed id:
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Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists.
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G.M.Alushin,
D.Jane,
M.L.Mayer.
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ABSTRACT
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The availability of crystal structures for the ligand binding domains of
ionotropic glutamate receptors, combined with their key role in synaptic
function in the normal and diseased brain, offers a unique selection of targets
for pharmaceutical research compared to other drug targets for which the atomic
structure of the ligand binding sites is not known. Currently only a few
antagonist structures have been solved, and these reveal ligand specific
conformational changes that hinder rational drug design. Here we report high
resolution crystal structures for three kainate receptor GluK1 antagonist
complexes which reveal new and unexpected modes of binding, highlighting the
continued need for experimentally determined receptor-ligand complexes.
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Links
