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Figure 1
A schematic of a heteropentameric GlyR. The stoichiometry is (α1)2(β)3, with the α1 subunit in red and the β subunit in cyan. Plus and minus symbols indicate the positions of the principal and complementary sides of the binding site, respectively. In this arrangement there are three types of binding site: two α1(+)/β(−), two α1(−)/β(+) and one β(+)/β(−). (b) Comparison of the loop segments that create the orthosteric ligand-binding sites in AcAChBP, human GlyR-α1 and GlyR-β. The residues colored red indicate where amino-acid substitutions have been carried out to create GBP. The four residues colored blue contribute to the binding site but have not been changed owing to structural conservation.

Volume 6| Part 6| November 2019| Pages 1014-1023
ISSN: 2052-2525