Molecular dynamics simulation of the 1:1 enzyme-ligand complex between porcine pancreatic elastase and acetyl-alanine-proline-alanine

✍ Scribed by T. Fujita; E. F. Meyer Jr.

• Publisher: John Wiley and Sons
• Year: 1987
• Tongue: English
• Weight: 630 KB
• Volume: 8
• Category: Article
• ISSN: 0192-8651
• DOI: 10.1002/jcc.540080608

✦ Synopsis

A 31.5 picosecond (ps) MD calculation has been completed for the 1 : 1 enzyme-ligand complex between porcine pancreatic elastase (PPE) and acetyl-alanine-proline-alanine (APA). The 1 : 2 complex studied crystallographically a t product saturation conditions precludes the study of a 1 : 1 complex (PPE and APA1); this objective has been achieved by computational methods described here. The acetyl group of the ligand was found to occupy two neighboring sites, one within the primary specificity site and the other out into solution. The primary change of the ligand structure is torsion angle being 171.5". Supported by an interactive graphic display, the dynamical fluctuations of a smaller ligand compared with the width of the active site as PPE were observed by the MD simulation, although the complex has not been detected by any spectroscopic method.