title: Ab initio fragment molecular orbital (FMO) method applied to analysis of the ligand-protein interaction in a pheromone-binding protein.
abstract: Full quantum computation of the electronic state of proteins has recently become possible by the advent of the ab initio fragment molecular orbital (FMO) method. We applied this method to the analysis of the interaction between the Bombyx mori pheromone-binding protein and its ligand, bombykol. The protein-ligand interaction of this molecular complex was minutely analyzed by the FMO method, and the analysis revealed several important interactions between the ligand and amino acid residues.
authors.affiliation: National Institute of Advanced Industrial Science and Technology, AIST Central 2, 1-1-1 Umezono, Tsukuba 305-8568, Japan.
authors.forename: Tadashi
authors.initials: T
authors.lastname: Nemoto
authors.forename: Dmitri G
authors.initials: DG
authors.lastname: Fedorov
authors.forename: Masami
authors.initials: M
authors.lastname: Uebayasi
authors.forename: Kenji
authors.initials: K
authors.lastname: Kanazawa
authors.forename: Kazuo
authors.initials: K
authors.lastname: Kitaura
authors.forename: Yuto
authors.initials: Y
authors.lastname: Komeiji
mesh_terms: D000818:Animals; D012831:Bombyx; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding
chemical_list: D002352:Carrier Proteins; D019476:Insect Proteins; D008024:Ligands; C403713:pheromone binding protein, insect