Mutational Analysis and Molecular Modeling of the Allosteric Binding Site of a Novel, Selective, Noncompetitive Antagonist of the Metabotropic Glutamate 1 Receptor*

@article{Malherbe2003MutationalAA,
  title={Mutational Analysis and Molecular Modeling of the Allosteric Binding Site of a Novel, Selective, Noncompetitive Antagonist of the Metabotropic Glutamate 1 Receptor*},
  author={Pari Malherbe and Nicole A. Kratochwil and Frédéric Knoflach and Marie‐Th{\'e}r{\`e}se Zenner and James N. C. Kew and Claudia Kratzeisen and H. P. Maerki and Geo Adam and Vincent Mutel},
  journal={The Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={8340 - 8347}
}
A model of the rmGlu1 seven-transmembrane domain complexed with a negative allosteric modulator, 1-ethyl-2-methyl-6-oxo-4-(1,2,4,5-tetrahydro-benzo[d]azepin-3-yl)- 1,6-dihydro-pyrimidine-5-carbonitrile (EM-TBPC) was constructed. Although the mGlu receptors belong to the family 3 G-protein-coupled receptors with a low primary sequence similarity to rhodopsin-like receptors, the high resolution crystal structure of rhodopsin was successfully applied as a template in this model and used to select… 

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