Ab initio fragment molecular orbital (FMO) method applied to analysis of the ligand-protein interaction in a pheromone-binding protein.
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.
Nemoto
Tadashi
T
National Institute of Advanced Industrial Science and Technology, AIST Central 2, 1-1-1 Umezono, Tsukuba 305-8568, Japan.
Fedorov
Dmitri G
DG
Uebayasi
Masami
M
Kanazawa
Kenji
K
Kitaura
Kazuo
K
Komeiji
Yuto
Y
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
D002352:Carrier Proteins; D019476:Insect Proteins; D008024:Ligands; C403713:pheromone binding protein, insect