In silico characterization of cytisinoids docked into an acetylcholine binding protein.

@article{AbinCarriquiry2010InSC,
  title={In silico characterization of cytisinoids docked into an acetylcholine binding protein.},
  author={Juan Andr{\'e}s Abin-Carriquiry and Margot Paulino Zunini and Bruce K. Cassels and Susan Wonnacott and Federico Dajas},
  journal={Bioorganic & medicinal chemistry letters},
  year={2010},
  volume={20 12},
  pages={3683-7}
}
Homology models of nicotinic acetylcholine receptors (nAChRs) suggest that subtype specificity is due to non-conserved residues in the complementary subunit of the ligand-binding pocket. Cytisine and its derivatives generally show a strong preference for heteromeric alpha4beta2* nAChRs over the homomeric alpha7 subtype, and the structural modifications studied do not cause large changes in their nAChR subtype selectivity. In the present work we docked cytisine, N-methylcytisine, and several… CONTINUE READING

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