[HTML][HTML] Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence
We delineated acetylcholine (ACh)-dependent conformational changes in a prototype of the
nicotinic receptor ligand binding domain by molecular dynamics simulation and changes in
intrinsic tryptophan (Trp) fluorescence. Prolonged molecular dynamics simulation of ACh-
binding protein showed that binding of ACh establishes close register of Trps from adjacent
subunits, Trp 143 and Trp 53, and draws the peripheral C-loop inward to occlude the
entrance to the binding cavity. Close register of Trp 143 and Trp 53 was demonstrated by …
nicotinic receptor ligand binding domain by molecular dynamics simulation and changes in
intrinsic tryptophan (Trp) fluorescence. Prolonged molecular dynamics simulation of ACh-
binding protein showed that binding of ACh establishes close register of Trps from adjacent
subunits, Trp 143 and Trp 53, and draws the peripheral C-loop inward to occlude the
entrance to the binding cavity. Close register of Trp 143 and Trp 53 was demonstrated by …
