The amino terminal domain (ATD) of the metabotropic glutamate (mGlu) receptors contains
the orthosteric glutamate recognition site, which is highly conserved across the eight mGlu receptor subtypes.
In total, 29 X-ray crystal structures of the mGlu ATD proteins have been reported to date. These
structures span across 3 subgroups and 6 subtypes, and include apo, agonist- and antagonist-bound structures.
We will discuss the insights gained from the analysis of these structures with the focus on the interactions
contributing to the observed group and subtype selectivity for select agonists. Furthermore,
we will define the full expanded orthosteric ligand binding pocket (LBP) of the mGlu receptors, and discuss
the macroscopic features of the mGlu ATD proteins.
Keywords: Class C GPCR, mGlu Receptor, Orthosteric ligand binding pocket, Structure-based drug design, Receptor activation.
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