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Protein Engineering, Vol. 15, No. 9, 717-720, September 2002
© 2002 Oxford University Press

COMMUNICATION

Ligand-specific conformations of an ionotropic glutamate receptor

Lajos Nyikos1, Ágnes Simon, Péter Barabás and Julianna Kardos

1 Department of Neurochemistry, Chemical Institute, Chemical Research Center, Hungarian Academy of Sciences, Pusztaszeri út 59–67, H-1025 Budapest, Hungary

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.


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