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PDBsum entry 3g3g

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protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
3g3g
Jmol
Contents
Protein chains
253 a.a. *
Ligands
GLU ×2
Metals
_NA ×2
_CL ×3
Waters ×663
* Residue conservation analysis
PDB id:
3g3g
Name: Membrane protein
Title: Crystal structure of the glur6 ligand binding domain dimer k665r mutant with glutamate and nacl at 1.3 angstrom resolution
Structure: Glutamate receptor, ionotropic kainate 2. Chain: a, b. Fragment: residues 429-544, 667-806. Synonym: glutamate receptor 6, glur-6, glur6. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Organism_taxid: 10116. Gene: grik2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.30Å     R-factor:   0.147     R-free:   0.168
Authors: C.Chaudhry,M.L.Mayer
Key ref: C.Chaudhry et al. (2009). Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization. EMBO J, 28, 1518-1530. PubMed id: 19339989
Date:
02-Feb-09     Release date:   02-Jun-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P42260  (GRIK2_RAT) -  Glutamate receptor ionotropic, kainate 2
Seq:
Struc:
 
Seq:
Struc:
908 a.a.
253 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  

 

 
EMBO J 28:1518-1530 (2009)
PubMed id: 19339989  
 
 
Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
C.Chaudhry, M.C.Weston, P.Schuck, C.Rosenmund, M.L.Mayer.
 
  ABSTRACT  
 
AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor ligand-binding domains form dimers, which are key functional units controlling ion-channel activation and desensitization. Dimer stability is inversely related to the rate and extent of desensitization. Kainate and AMPA receptors share common structural elements, but functional measurements suggest that subunit assembly and gating differs between these subtypes. To investigate this, we constructed a library of GluR6 kainate receptor mutants and directly measured changes in kainate receptor dimer stability by analytical ultracentrifugation, which, combined with electrophysiological experiments, revealed an inverse correlation between dimer stability and the rate of desensitization. We solved crystal structures for a series of five GluR6 mutants, to understand the molecular mechanisms for dimer stabilization. We demonstrate that the desensitized state of kainate receptors acts as a deep energy well offsetting the stabilizing effects of dimer interface mutants, and that the deactivation of kainate receptor responses is dominated by entry into desensitized states. Our results show how neurotransmitter receptors with similar structures and gating mechanisms can exhibit strikingly different functional properties.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21372852 M.L.Mayer (2011).
Glutamate receptor ion channels: where do all the calories go?
  Nat Struct Mol Biol, 18, 253-254.  
21349697 M.L.Mayer (2011).
Structure and mechanism of glutamate receptor ion channel assembly, activation and modulation.
  Curr Opin Neurobiol, 21, 283-290.  
21167941 R.Ghirlando (2011).
The analysis of macromolecular interactions by sedimentation equilibrium.
  Methods, 54, 145-156.  
20881961 T.Nogi, N.Yasui, E.Mihara, Y.Matsunaga, M.Noda, N.Yamashita, T.Toyofuku, S.Uchiyama, Y.Goshima, A.Kumanogoh, and J.Takagi (2010).
Structural basis for semaphorin signalling through the plexin receptor.
  Nature, 467, 1123-1127.
PDB codes: 3afc 3al8 3al9
20404149 U.Das, J.Kumar, M.L.Mayer, and A.J.Plested (2010).
Domain organization and function in GluK2 subtype kainate receptors.
  Proc Natl Acad Sci U S A, 107, 8463-8468.  
19617541 C.Chaudhry, A.J.Plested, P.Schuck, and M.L.Mayer (2009).
Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.
  Proc Natl Acad Sci U S A, 106, 12329-12334.  
19561126 N.Nayeem, Y.Zhang, D.K.Schweppe, D.R.Madden, and T.Green (2009).
A nondesensitizing kainate receptor point mutant.
  Mol Pharmacol, 76, 534-542.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.