The binding mode of an E-64 analog to the active site of cathepsin B

Two binding modes of the isobutyl-NH-Eps-Leu-Pro inhibitor to cathepsin B have been proposed. Molecular docking using an empirical force field was carried out to distinguish between the two modes. The search began with manual docking, followed by random perturbations of the docking conformation and...

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Veröffentlicht in:	Protein engineering 1996-11, Vol.9 (11), p.977-986
Hauptverfasser:	Feng, Ming-Hsiang, Chan, Shek Ling, Xiang, Yuefang, Huber, Carol P., Lim, Carmay
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites cathepsin B Cathepsin B - antagonists & inhibitors Cathepsin B - chemistry Cathepsin B - metabolism Computer Simulation conformational search cysteine protease Cysteine Proteinase Inhibitors - chemistry Cysteine Proteinase Inhibitors - metabolism Dipeptides - chemistry Hydrogen Bonding inhibitors Leucine - analogs & derivatives Leucine - chemistry Leucine - metabolism Models, Molecular Molecular Conformation molecular dynamics Monte Carlo Method Structure-Activity Relationship
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