The first group gathers five residues at both M1( − ) and M3( + ) helices, whose mutations have highly significant effects on the GlyR potentiation (hS241, hW243, hF295, hL298, and hL299) and clearly highlight the lower intersubunit binding site identified by CG/MD (red).
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A millisecond coarse-grained simulation approach to decipher allosteric cannabinoid binding at the glycine receptor α1.
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