Crystal Structure of Lymnaea stagnalis Acetylcholine Binding Protein Complexed with Thiacloprid

Studies on an acetylcholine binding protein identify a basic residue in loop G on the beta 1 strand as a new structural determinant of neonicotinoid actions

0.2M Na citrate pH 5.7, 15-22% PEG3350, 0.5mM thiacloprid, VAPOR DIFFUSION, temperature 293K

AUTHORS STATE THAT BEFORE CRYSTALLIZATION, THE N-GLUCOSIDE GROUPS WERE REMOVED BY PEPTIDE-N-GLYCOSIDASE F. THE CONFLICT IS DUE TO POST-TRANSLATIONAL MODIFICATION AND SAMPLE PREPARATION.

neonicotinoids, nicotinic acetylcholine receptor, thiacloprid, acetylcholine binding, SIGNALING PROTEIN