Emerging the role of the structure of brain membrane targets recognizing glutamate

Ágnes Simon, Ákos Bencsura, Anna Palló, László Héja, Julianna Kardos

Research output: Contribution to journalReview article

1 Citation (Scopus)

Abstract

Ligand-bound and free structures of brain membrane targets for L-glutamate (Glu) suggest the view, that quaternary rearrangements are associated with ligand binding. Rearrangement of the machinery of the signaling apparatus, such as molecular switches, recognition sites and the target structures for ligand binding of Glu-operated ion channel and heptahelical G-protein-coupled family receptors have been quantified and compared with the use of the root mean square (RMS) values. In addition to conformational rearrangement of the Glu receptor structures in complex with a series of ligands, conformations of Glu in various target structures became available. High resolution data revealed that the extended Glu conformation is conserved in the binding crevice of all ionotropic Glu receptors (iGluRs). Furthermore, the extended conformations of Glu that characterize iGluRs and mGluRs are distinguishable by distance and torsion angle parameters, such as δC1-C2 and Cα-Cβ-Cγ-C2. By contrast, a bent Glu conformation is recognized in Glu transporters.

Original languageEnglish
Pages (from-to)70-74
Number of pages5
JournalCurrent drug discovery technologies
Volume5
Issue number1
DOIs
Publication statusPublished - Mar 1 2008

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Keywords

  • Glutamate conformation
  • Glutamate transporter
  • Ionotropic glutamate receptor
  • Metabotropic glutamate receptor
  • PDB database analysis

ASJC Scopus subject areas

  • Drug Discovery

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