title: Molecular structure of FR901277, a novel inhibitor of human leukocyte elastase, and its binding mode simulation.
abstract: X-ray crystal structure analysis of FR901277, a novel inhibitor of human leukocyte elastase, was performed and revealed that the lipophilic side chains are located towards the outside of the molecule. Binding simulation using computational methods showed that these lipophilic moieties could bind to the hydrophobic binding pockets of HLE.
authors.affiliation: Basic Research Laboratories, Fujisawa Pharmaceutical Co., Ltd., Osaka, Japan.
authors.forename: I
authors.initials: I
authors.lastname: Nakanishi
authors.forename: T
authors.initials: T
authors.lastname: Kinoshita
authors.forename: T
authors.initials: T
authors.lastname: Tada
authors.forename: T
authors.initials: T
authors.lastname: Fujita
authors.forename: H
authors.initials: H
authors.lastname: Hatanaka
authors.forename: A
authors.initials: A
authors.lastname: Sato
mesh_terms: D000577:Amides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding
chemical_list: D000577:Amides; D004791:Enzyme Inhibitors; C120193:FR 901277; D019272:Leukocyte Elastase