MOLECULAR-MODEL OF THE SPECIFICITY POCKET OF THE HEPATITIS-C VIRUS PROTEASE - IMPLICATIONS FOR SUBSTRATE RECOGNITION

被引：93

作者：

PIZZI, E

TRAMONTANO, A

TOMEI, L

LAMONICA, N

FAILLA, C

SARDANA, M

WOOD, T

DEFRANCESCO, R

机构：

[1] IST RIC BIOL MOLEC,P ANGELETTI POMEZIA,I-00040 ROME,ITALY

[2] MERCK SHARP & DOHME LTD,W POINT,PA 19486

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 03期

关键词：

MODEL BUILDING; NONSTRUCTURAL PROTEIN NS3; N-TERMINAL SEQUENCING; SEQUENCE ALIGNMENT;

D O I：

10.1073/pnas.91.3.888

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We have built a model of the specificity pocket of the protease of hepatitis C virus on the basis of the known structures of trypsin-like serine proteases and of the conservation pattern of the protease sequences among various hepatitis C strains. The model allowed us to predict that the substrate of this protease should have a cysteine residue in position Pl. This hypothesis was subsequently proved by N-terminal sequencing of two products of the protease. The success of this ''blind'' test increases our confidence in the overall correctness of our proposed alignment of the enzyme sequence with those of other proteases of known structure and constitutes a first step in the construction of a complete model of the viral protease domain.

引用

页码：888 / 892

页数：5

共 44 条

[1] DETECTION OF A TRYPSIN-LIKE SERINE PROTEASE DOMAIN IN FLAVIVIRUSES AND PESTIVIRUSES [J].