Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the nicotinic acetylcholine receptor.

@article{Dutertre2005Beta2SC,
  title={Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the nicotinic acetylcholine receptor.},
  author={S{\'e}bastien Dutertre and Annette Nicke and Richard J Lewis},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 34},
  pages={30460-8}
}
The structures of acetylcholine-binding protein (AChBP) and nicotinic acetylcholine receptor (nAChR) homology models have been used to interpret data from mutagenesis experiments at the nAChR. However, little is known about AChBP-derived structures as predictive tools. Molecular surface analysis of nAChR models has revealed a conserved cleft as the likely binding site for the 4/7 alpha-conotoxins. Here, we used an alpha3beta2 model to identify beta2 subunit residues in this cleft and… CONTINUE READING