The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site

During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 Å resolution....

Full description

Saved in:
Bibliographic Details
Published in:Cell 1996-10, Vol.87 (2), p.331-342
Main Authors: Love, Robert A, Parge, Hans E, Wickersham, John A, Hostomsky, Zdenek, Habuka, Noriyuki, Moomaw, Ellen W, Adachi, Tsuyoshi, Hostomska, Zuzana
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Hepatitis C - enzymology
hepatitis C virus
Metalloproteins - ultrastructure
Models, Molecular
Molecular Sequence Data
Recombinant Proteins
Sequence Alignment
Trypsin
Viral Nonstructural Proteins - ultrastructure
Zinc
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 Å resolution. NS3P folds as a trypsin-like proteinase with two β barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage specificity of the enzyme. Novel features include a structural zinc-binding site and a long N-terminus that interacts with neighboring molecules by binding to a hydrophobic surface patch.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)81350-1