Glutamate receptors at atomic resolution

Nature. 2006 Mar 23;440(7083):456-62. doi: 10.1038/nature04709.


At synapses throughout the brain and spinal cord, the amino-acid glutamate is the major excitatory neurotransmitter. During evolution, a family of glutamate-receptor ion channels seems to have been assembled from a kit consisting of discrete ligand-binding, ion-channel, modulatory and cytoplasmic domains. Crystallographic studies that exploit this unique architecture have greatly aided structural analysis of the ligand-binding core, but the results also pose a formidable challenge, namely that of resolving the allosteric mechanisms by which individual domains communicate and function in an intact receptor.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Allosteric Regulation
  • Amino Acid Sequence
  • Animals
  • Excitatory Amino Acid Agonists / metabolism
  • Excitatory Amino Acid Agonists / pharmacology
  • Forecasting
  • Glutamic Acid / genetics
  • Glutamic Acid / metabolism
  • Humans
  • Ion Channels / chemistry
  • Ion Channels / metabolism
  • Ligands
  • Molecular Sequence Data
  • Neurodegenerative Diseases / metabolism
  • Receptors, AMPA / chemistry
  • Receptors, AMPA / metabolism
  • Receptors, Glutamate / chemistry*
  • Receptors, Glutamate / metabolism


  • Excitatory Amino Acid Agonists
  • Ion Channels
  • Ligands
  • Receptors, AMPA
  • Receptors, Glutamate
  • Glutamic Acid