PDBsum entry 3bft

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protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
Protein chains
259 a.a. *
S2P ×3
_NA ×2
_ZN ×5
Waters ×568
* Residue conservation analysis
PDB id:
Name: Membrane protein
Title: Structure of the ligand-binding core of glur2 in complex wit agonist (s)-tdpa at 2.25 a resolution
Structure: Glutamate receptor 2. Chain: a, b, c. Fragment: residues 1-263. Synonym: glur-2, glur-b, glur-k2, glutamate receptor ionotr 2, ampa-selective glutamate receptor 2. Engineered: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: gria2, glur2. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.27Å     R-factor:   0.200     R-free:   0.250
Authors: M.Beich-Frandsen,O.Mirza,B.Vestergaard,M.Gajhede,J.S.Kastrup
Key ref: 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: 18269227 DOI: 10.1021/jm701126w
23-Nov-07     Release date:   28-Oct-08    
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Protein chains
Pfam   ArchSchema ?
P19491  (GRIA2_RAT) -  Glutamate receptor 2
883 a.a.
259 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     transport   1 term 
  Biochemical function     transporter activity     3 terms  


DOI no: 10.1021/jm701126w J Med Chem 51:1459-1463 (2008)
PubMed id: 18269227  
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.
M.Beich-Frandsen, D.S.Pickering, O.Mirza, T.N.Johansen, J.Greenwood, B.Vestergaard, A.Schousboe, M.Gajhede, T.Liljefors, J.S.Kastrup.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20713069 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.
  Neuropharmacology, 60, 135-150.  
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