The structures of picornaviral proteinases

被引:94
作者
Seipelt, J
Guarné, A
Bergmann, E
James, M
Sommergruber, W
Fita, I
Skern, T
机构
[1] Univ Vienna, Inst Biochem, Fac Med, A-1030 Vienna, Austria
[2] Ctr Invest Desenvolupament, CSIC, E-08034 Barcelona, Spain
[3] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2H7, Canada
[4] Bender & Co, Dept Cell Biol, Boehringer Ingelheim Res, A-1120 Vienna, Austria
基金
奥地利科学基金会;
关键词
picornaviruses; proteolytic activities; three-dimensional structures;
D O I
10.1016/S0168-1702(99)00043-X
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Picornaviruses are a family of positive-strand RNA viruses the members of which include poliovirus, hepatitis A virus, rhinovirus, foot-and-mouth disease virus and encephalomyocarditis virus. The genetic information contained in the single-stranded, positive sense RNA genome is expressed as a single protein of around 2000 amino acids. This primary product of protein synthesis, designated the polyprotein, is subsequently cleaved into the mature viral proteins by proteinases present within it. The properties of the three defined proteolytic activities present in the picornaviruses are reviewed and the three-dimensional structures of the hepatitis A 3C proteinase and the leader proteinase of foot-and-mouth disease virus as well as a model of the structure of the HRV2 2A proteinase are compared with those of chymotrypsin, papain and streptomyces griseus A proteinase, respectively. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:159 / 168
页数:10
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