Summary of alanine-scanning mutagenesis for homologous contact residues in the α1 GlyR and α7 nAChR.

The two-electrode voltage clamp technique was used to measure the affinity of strychnine on d-TC for mutants of the α1 GlyR and α7 nAChR, respectively. Structure-based sequence alignments were calculated and residues homologous to those involved in ligand interactions in AChBP structures were mutated to Ala. The Ala residue at position 101 in the α1 GlyR (homologous to Y91 in Ac-AChBP) was mutated to F. NC, no current.aResidues that form unique contacts with strychnine in double ligand occupancy mode.bIC50-values obtained from Grudzinska et al. [23].