Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate

FEBS Lett. 2005 Feb 14;579(5):1154-60. doi: 10.1016/j.febslet.2005.01.012.

Abstract

The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95 A resolution. The overall GluR5-S1S2 structure comprises two domains and is similar to the related AMPA receptor GluR2-S1S2J. (S)-glutamate binds as in GluR2-S1S2J. Distinct features are observed for Ser741, which stabilizes a highly coordinated network of water molecules and forms an interdomain bridge. The GluR5 complex exhibits a high degree of domain closure (26 degrees) relative to apo GluR2-S1S2J. In addition, GluR5-S1S2 forms a novel dimer interface with a different arrangement of the two protomers compared to GluR2-S1S2J.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Dimerization
  • Glutamates / metabolism*
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Receptors, AMPA / chemistry
  • Receptors, AMPA / metabolism
  • Receptors, Kainic Acid / chemistry*
  • Receptors, Kainic Acid / metabolism*
  • Sequence Alignment

Substances

  • Gluk1 kainate receptor
  • Glutamates
  • Ligands
  • Receptors, AMPA
  • Receptors, Kainic Acid
  • glutamate receptor ionotropic, AMPA 2