rhmGluR8, CF (100 UG)

Background: mGluR8

Metabotropic glutamate receptors (mGluRs) are members of the G-protein-coupled receptor (GPCR) superfamily, modulating glutamate neurotransmission in the central and peripheral nervous systems through GTP-binding proteins (1). Structurally, members of this family are characterized by a large N-terminal extracellular domain (ECD), seven transmembrane domains, and a cytoplasmic C-terminal domain that is variable in length. Two ECDs dimerize together and large conformational changes are induced when agonists bind to one or both domains (2). The C-terminal region is subject to alternative splicing, regulation by phosphorylation, and interacts directly with a G-protein to modulate protein-protein interactions (2, 3). The receptors are subdivided into three groups (I–III) based on sequence homology, signal transduction and pharmacological properties (1, 2). The Group III receptors include mGLuRs 4, 6, 7 and 8 (2). Mature human mGluR8 is 875 amino acids in length, including a 550 amino acid (aa) N-terminal ECD (4). Within N-terminal ECD, human mGluR8 shares 98.4% and 98.5% aa sequence identity with mouse and rat mGluR8, respectively.