2zjv

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Revision as of 11:22, 9 April 2008

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Template:STRUCTURE 2zjv

Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein (Ls-AChBP) Complexed with Clothianidin

Overview

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 that the guanidine moiety of IMI and CTD stacks with Tyr185, while the nitro group of IMI but not of CTD makes a hydrogen bond with Gln55. IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH-pi interactions in the Ls-AChBP-CTD complex than in the Ls-AChBP-IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD. Yet, the NH at position 1 of CTD makes a hydrogen bond with the backbone carbonyl of Trp143, offering an explanation for the diverse actions of neonicotinoids on nAChRs.

About this Structure

2ZJV is a Single protein structure of sequence from Lymnaea stagnalis. Full crystallographic information is available from OCA.

Reference

Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin., Ihara M, Okajima T, Yamashita A, Oda T, Hirata K, Nishiwaki H, Morimoto T, Akamatsu M, Ashikawa Y, Kuroda S, Mega R, Kuramitsu S, Sattelle DB, Matsuda K, Invert Neurosci. 2008 Mar 13;. PMID:18338186