Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

@article{Ihara2008CrystalSO,
  title={Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin},
  author={Makoto Ihara and Toshihide Okajima and Atsuko Yamashita and Takuma Oda and Koichi Hirata and Hisashi Nishiwaki and Takako Morimoto and Miki Akamatsu and Yuji Ashikawa and Shun’ichi Kuroda and Ryosuke Mega and Seiki Kuramitsu and David B Sattelle and Kazuhiko Matsuda},
  journal={Invertebrate Neuroscience },
  year={2008},
  volume={8},
  pages={71 - 81}
}
Neonicotinoid insecticides, which act on nicotinic acetylcholine receptors (nAChRs) in a variety of ways, have extremely low mammalian toxicity, yet the molecular basis of such actions is poorly understood. To elucidate the molecular basis for nAChR–neonicotinoid interactions, a surrogate protein, acetylcholine binding protein from Lymnaea stagnalis (Ls-AChBP) was crystallized in complex with neonicotinoid insecticides imidacloprid (IMI) or clothianidin (CTD). The crystal structures suggested… CONTINUE READING
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