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The function of the amino terminal domain in NMDA receptor modulation

  • University of Oxford
Research Output:
Contribution to journal
Article
 Peer-review

Abstract

The authors have modelled dimers of the amino terminal domains of these receptors based on their homology with the extracellular dimer of a metabotropic glutamate receptor. Conserved cysteine residues, which have been highlighted as important in previous work, are shown to form a disulphide bridge, stabilizing a four-helix bundle between subunits. This establishes a hinge in the receptor. The model also highlights a zinc binding site in the binding crevice of the NR2a subunit of the receptor that stabilizes the open state of the amino terminal domain. The similar effect of ifenprodil is thus explained by its stabilization of the open state of the amino terminal domain (ATD). The presence of three histidine residues in the zinc site is used to explain the pH dependence of zinc inhibition.

Publication Information

Output type

Research Output:
Contribution to journal
Article
 Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 381-388

Journal (Volume, Issue Number)

Journal of Molecular Graphics and Modelling (Volume 23, Issue 4)

Publication milestones

  • Published - 01/01/2005

Publication status

Published - 01/01/2005

ISSN

1093-3263

Publication IDs

  • handle.net: 10547/294525
  • Scopus: 12844268621

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