Molecular structure of FR901277, a novel inhibitor of human leukocyte elastase, and its binding mode simulation.
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.
Nakanishi
I
I
Basic Research Laboratories, Fujisawa Pharmaceutical Co., Ltd., Osaka, Japan.
Kinoshita
T
T
Tada
T
T
Fujita
T
T
Hatanaka
H
H
Sato
A
A
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
D000577:Amides; D004791:Enzyme Inhibitors; C120193:FR 901277; D019272:Leukocyte Elastase