Ligand-specific conformations of an ionotropic glutamate receptor

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A simple in silico procedure is proposed with a view to predict the agonist or antagonist character of new, AMPA-type Glu receptor channel ligands. Based on the experimental binding domain structures, the orientation of a single Lys residue close to the ligand binding core was found to be diagnostic of ligand-induced conformational changes. Acting as a switch, the position of the Lys residue indicates the agonist or antagonist character of AMPA receptor ligands, known to bind to the receptor. Stability centre analysis substantiated the key role this switch might play in ligand-induced conformational changes.

Original languageEnglish
Pages (from-to)717-720
Number of pages4
JournalProtein Engineering
Volume15
Issue number9
Publication statusPublished - Sep 1 2002

Keywords

  • 3D Pharmacophore
  • Lysine switch
  • Rational drug design
  • Stabilization centres

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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