Mutational analysis and molecular modeling of the binding pocket of the metabotropic glutamate 5 receptor negative modulator 2-methyl-6-(phenylethynyl)-pyridine.

@article{Malherbe2003MutationalAA,
  title={Mutational analysis and molecular modeling of the binding pocket of the metabotropic glutamate 5 receptor negative modulator 2-methyl-6-(phenylethynyl)-pyridine.},
  author={Pari Malherbe and Nicole A. Kratochwil and Marie‐Th{\'e}r{\`e}se Zenner and Jenny Piussi and Catherine Diener and Claudia Kratzeisen and Christophe Fischer and Richard H. P. Porter},
  journal={Molecular pharmacology},
  year={2003},
  volume={64 4},
  pages={
          823-32
        }
}
Metabotropic glutamate (mGlu) 5 is a G-protein-coupled metabotropic glutamate receptor that plays an important role as a modulator of synaptic plasticity, ion channel activity, and excitotoxicity. 2-Methyl-6-(phenylethynyl)-pyridine (MPEP) is a highly potent, noncompetitive, selective, and systemically active antagonist of mGlu5 receptors. It binds to a novel allosteric site that resides within the seven-transmembrane domain of mGlu5 receptors. Using site-directed mutagenesis, [3H]MPEP binding… 

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