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PDBsum entry 3bfu
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Membrane protein
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PDB id
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3bfu
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Contents |
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* Residue conservation analysis
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PDB id:
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Membrane protein
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Title:
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Structure of the ligand-binding core of glur2 in complex with the agonist (r)-tdpa at 1.95 a resolution
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Structure:
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Glutamate receptor 2. Chain: a, b, c, d. Fragment: residues 1-263. Synonym: glur-2, glur-b, glur-k2, glutamate receptor ionotropic, ampa 2, ampa-selective glutamate receptor 2. Engineered: yes
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: gria2, glur2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.95Å
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R-factor:
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0.200
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R-free:
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0.233
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Authors:
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M.Beich-Frandsen,O.Mirza,B.Vestergaard,M.Gajhede,J.S.Kastrup
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Key ref:
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M.Beich-Frandsen
et al.
(2008).
Structures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotency.
J Med Chem,
51,
1459-1463.
PubMed id:
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Date:
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23-Nov-07
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Release date:
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14-Oct-08
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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.
262 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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J Med Chem
51:1459-1463
(2008)
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PubMed id:
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Structures of the ligand-binding core of iGluR2 in complex with the agonists (R)- and (S)-2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid explain their unusual equipotency.
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M.Beich-Frandsen,
D.S.Pickering,
O.Mirza,
T.N.Johansen,
J.Greenwood,
B.Vestergaard,
A.Schousboe,
M.Gajhede,
T.Liljefors,
J.S.Kastrup.
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ABSTRACT
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AMPA-type ionotropic glutamate receptors generally display high
stereoselectivity in agonist binding. However, the stereoisomers of
2-amino-3-(4-hydroxy-1,2,5-thiadiazol-3-yl)propionic acid (TDPA) have similar
enantiopharmacology. To understand this observation, we have determined the
X-ray structures of ( R)-TDPA and ( S)-TDPA in complex with the ligand-binding
core of iGluR2 and investigated the binding pharmacology at AMPA and kainate
receptors. Both enantiomers induce full domain closure in iGluR2 but adopt
different conformations when binding to the receptor, which may explain the
similar enantiopharmacology.
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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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J.Pøhlsgaard,
K.Frydenvang,
U.Madsen,
and
J.S.Kastrup
(2011).
Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators.
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Neuropharmacology,
60,
135-150.
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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.
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Links
