The amino terminal domain (ATD) of metabotropic glutamate receptors (mGluRs) contains the neurotransmitter binding site and is related in sequence to leucine/isoleucine/valine binding proteins (LIVBP). It has been proposed that the ATD of mGluRs shares with periplasmic binding proteins a common mechanism of ligand binding and processing which involves the equilibrium between closed and open forms. The availability of the X-ray structure of LIVBP in its open, unliganded form, has allowed the construction of homology models of the ATD of mGluR1 which have been instrumental in clarifying the mode of binding of agonists and antagonists. We propose in this paper the use of the X-ray structure of AmiC. the controller of transcription antitermination in the amidiase operon of Pseudomonas aerugimosa as suitable template for the construction of the closed form of the ATD of mGluR1. The resulting model of the closed form of the ATD of mGluR1 indicates that several interdomain hydrogen bonds and salt bridges may be formed upon domain contraction and that the ligand directly participates to this interdomain network.