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PDBsum entry 2qs1

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protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
2qs1
Jmol
Contents
Protein chains
251 a.a. *
Ligands
1PE ×2
UB1 ×2
Metals
_CL ×2
Waters ×366
* Residue conservation analysis
PDB id:
2qs1
Name: Membrane protein
Title: Crystal structure of the glur5 ligand binding core dimer in with ubp315 at 1.80 angstroms resolution
Structure: Glutamate receptor, ionotropic kainate 1. Chain: a, b. Synonym: glutamate receptor 5, glur-5, glur5. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: grik1, glur5. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.199     R-free:   0.219
Authors: G.M.Alushin,D.E.Jane,M.L.Mayer
Key ref: 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: 20558186
Date:
30-Jul-07     Release date:   05-Aug-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P22756  (GRIK1_RAT) -  Glutamate receptor ionotropic, kainate 1
Seq:
Struc:
 
Seq:
Struc:
949 a.a.
251 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biochemical function     ionotropic glutamate receptor activity     2 terms  

 

 
Neuropharmacology 60:126-134 (2011)
PubMed id: 20558186  
 
 
Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists.
G.M.Alushin, D.Jane, M.L.Mayer.
 
  ABSTRACT  
 
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.