High Level Production, Characterization and Construct Optimization of the Ionotropic Glutamate Receptor Ligand Binding Core

Multimilligram quantities of active and pure GluR2-S1S2, the recombinant ligand binding core of the AMPA-sensitive GluR2 receptor, were produced by preparative folding of the solubilized inclusion bodies expressed in 1 l of Escherichia coli cell culture. The biochemical properties and biological activities of folded protein were characterized and the protein construct was optimized for three-dimensional structural studies.