The solution structure of the hepatitis C virus (BK strain) NS3 protein N-terminal domain (186 residues) has been solved by NMR spectroscopy. The protein is a serine protease with a chymotrypsin-type fold, and is involved in the maturation of the viral polyprotein. Despite the knowledge that its activity is enhanced by the action of a viral protein cofactor, NS4A, the mechanism of activation is not yet clear. The analysis of the folding in solution and the differences from the crystallographic structures allow the formulation of a model in which, in addition to the NS4A cofactor, the substrate plays an important role in the activation of the catalytic mechanism. A unique structural feature is the presence of a zinc-binding site exposed on the surface, subject to a slow conformational exchange process.

Barbato, G., Cicero, D.o., Nardi, M., Steinkuhler, C., Cortese, R., De Francesco, R., et al. (1999). The solution structure of the N-terminal proteinase domain of the Hepatitis C Virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. JOURNAL OF MOLECULAR BIOLOGY, 289, 371-384.

The solution structure of the N-terminal proteinase domain of the Hepatitis C Virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism

CICERO, DANIEL OSCAR;
1999-01-01

Abstract

The solution structure of the hepatitis C virus (BK strain) NS3 protein N-terminal domain (186 residues) has been solved by NMR spectroscopy. The protein is a serine protease with a chymotrypsin-type fold, and is involved in the maturation of the viral polyprotein. Despite the knowledge that its activity is enhanced by the action of a viral protein cofactor, NS4A, the mechanism of activation is not yet clear. The analysis of the folding in solution and the differences from the crystallographic structures allow the formulation of a model in which, in addition to the NS4A cofactor, the substrate plays an important role in the activation of the catalytic mechanism. A unique structural feature is the presence of a zinc-binding site exposed on the surface, subject to a slow conformational exchange process.
1999
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10 - BIOCHIMICA
English
Barbato, G., Cicero, D.o., Nardi, M., Steinkuhler, C., Cortese, R., De Francesco, R., et al. (1999). The solution structure of the N-terminal proteinase domain of the Hepatitis C Virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. JOURNAL OF MOLECULAR BIOLOGY, 289, 371-384.
Barbato, G; Cicero, Do; Nardi, M; Steinkuhler, C; Cortese, R; De Francesco, R; Bazzo, R
Articolo su rivista
File in questo prodotto:
File Dimensione Formato  
2_1_19.pdf

accesso aperto

Dimensione 654.06 kB
Formato Adobe PDF
654.06 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/87875
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 104
  • ???jsp.display-item.citation.isi??? 102
social impact