NMR conformational studies on a synthetic peptide reproducing the [1-20] processing domain of the pro-ocytocin-neurophysin precursor

✍ Scribed by Lucia Falcigno; Livio Paolillo; Gabriella D'Auria; Michele Saviano; Mario Simonetti; Carlo Di Bello

• Publisher: Wiley (John Wiley & Sons)
• Year: 1998
• Tongue: English
• Weight: 861 KB
• Volume: 39
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(199612)39:6<837::aid-bip8>3.0.co;2-w

✦ Synopsis

The combined use of several nuclear magnetic resonance and restrained molecular dynamics techniques allowed the formulation of a molecular model for the preferred solution conformation of a synthetic peptide reproducing the [ 1-20] processing domain of thepro-ocytocin-neurophysin precursor. In the model, the conformation of the 20-membered tocin ring, with the two Cys' and Cys6 residues bridged by a disulphide bond, is very close to that observed for isolated ocytocin in the solid state; in addition, a type II &turn is postulated for the 7-10 segment of the acyclic tail containing the Lys"-Arg'2 processing site, and connecting ocytocin to the neurophysin domain, while the C-terminall3-20 segment of the molecule is believed to assume a helical structure. This particular structural organization could be important in participating as the favorable conformation for optimal substrate-enzyme active site recognition and processing by specific endoproteases.