title: Acetylcholinesterase: enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2.
abstract: A 15 ns molecular dynamics simulation is reported for the complex of mouse acetylcholinesterase (mAChE) and the protein neurotoxin fasciculin-2. As compared to a 15 ns simulation of apo-mAChE, the structural fluctuations of the enzyme are substantially increased in magnitude for the enzyme in the complex. Fluctuations of part of the long omega loop (residues 69-96) are particularly enhanced. This loop forms one wall of the active site, and the enhanced fluctuations lead to additional routes of access to the active site.
authors.affiliation: Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0365, USA. jbui@mccammon.ucsd.edu
authors.forename: Jennifer M
authors.initials: JM
authors.lastname: Bui
authors.forename: Kaihsu
authors.initials: K
authors.lastname: Tai
authors.forename: J Andrew
authors.initials: JA
authors.lastname: McCammon
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry* / Q000378:metabolism*; D000215:Acylation; D001665:Binding Sites; D004546:Elapid Venoms / Q000737:chemistry* / Q000378:metabolism*; D005454:Fluorescence Polarization; D008958:Models, Molecular; D018583:Pliability; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D004546:Elapid Venoms; C044937:fasciculin; D000110:Acetylcholinesterase