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The cloning and molecular characterization of a heterodimeric G-protein-coupled receptor for divalent cations which has been designated as mGluR2 is described. It is a 90 kDa receptor, whose amino-terminus bears homology with mGluR1, and whose carboxy-terminus is homologous with N-terminal sequences of mGluR3/4. The ligand-binding site of this receptor consists of a relatively conserved Asp (D) residue situated in the third position of the putative ligand-binding motif Asp-X-Gly-X-Asp-Ser-X-Gly-Leu-X (SEQ ID NO:1). Two of the Asp residues can be substituted by a glutamate or a leucine residue in case of an Asp–>Glu or Asp–>Leu mutation. In contrast to mGluR1, mGluR2 can be coupled efficiently to G proteins from Rho as well as Go.# Lines starting with ‘#’ and sections without content
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