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PDBsum entry 3fas

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protein ligands Protein-protein interface(s) links
Membrane protein PDB id
3fas

 

 

 

 

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Contents
Protein chains
260 a.a. *
Ligands
GLU ×2
SO4 ×8
GOL ×9
Waters ×888
* Residue conservation analysis
PDB id:
3fas
Name: Membrane protein
Title: X-ray structure of iglur4 flip ligand-binding core (s1s2) in complex with (s)-glutamate at 1.40a resolution
Structure: Glutamate receptor 4. Chain: a, b. Fragment: iglur4 flip ligand-binding core (s1s2). Synonym: ionotropic glutamate receptor 4, glur-4, glur4, glur-d, glutamate receptor ionotropic, ampa 4, ampa-selective glutamate receptor 4. Engineered: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.40Å     R-factor:   0.167     R-free:   0.183
Authors: C.Kasper,K.Frydenvang,P.Naur,M.Gajhede,J.S.Kastrup
Key ref: C.Kasper et al. (2008). Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4. Febs Lett, 582, 4089-4094. PubMed id: 19022251
Date:
18-Nov-08     Release date:   09-Dec-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P19493  (GRIA4_RAT) -  Glutamate receptor 4 from Rattus norvegicus
Seq:
Struc:
 
Seq:
Struc:
902 a.a.
260 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 10 residue positions (black crosses)

 

 
Febs Lett 582:4089-4094 (2008)
PubMed id: 19022251  
 
 
Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4.
C.Kasper, K.Frydenvang, P.Naur, M.Gajhede, D.S.Pickering, J.S.Kastrup.
 
  ABSTRACT  
 
The alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) class of ionotropic glutamate receptors comprises four different subunits: iGluR1/iGluR2 and iGluR3/iGluR4 forming two subgroups. Three-dimensional structures have been reported only of the ligand-binding core of iGluR2. Here, we present two X-ray structures of a soluble construct of the R/G unedited flip splice variant of the ligand-binding core of iGluR4 (iGluR4(i)(R)-S1S2) in complex with glutamate or AMPA. Subtle, but important differences are found in the ligand-binding cavity between the two AMPA receptor subgroups at position 724 (Tyr in iGluR1/iGluR2 and Phe in iGluR3/iGluR4), which in iGluR4 may lead to displacement of a water molecule and hence points to the possibility to make subgroup specific ligands.
 

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.  
21349697 M.L.Mayer (2011).
Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.
  Curr Opin Neurobiol, 21, 283-290.  
20856958 R.Vijayan, M.A.Sahai, T.Czajkowski, and P.C.Biggin (2010).
A comparative analysis of the role of water in the binding pockets of ionotropic glutamate receptors.
  Phys Chem Chem Phys, 12, 14057-14066.  
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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