Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA

被引：24

作者：

Mangel, WF

Toledo, DL

Ding, JZ

Sweet, RM

McGrath, WJ

机构：

[1] Biology Department, Brookhaven National Laboratory, Upton

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1997年 / 22卷 / 10期

关键词：

D O I：

10.1016/S0968-0004(97)01123-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The adenovirus proteinase (AVP) uses both an Il-amino acid peptide (pVlC)(1,2) and the viral DNA(1) as cofactors to increase its catalytic rate constant 6000-fold. The crystal structure(3) of an AVP-pVlc complex at 2.6-Angstrom resolution reveals a new protein fold of an enzyme that is the first member of a new class of cysteine proteinases, which arose via convergent evolution.

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页码：393 / 398

页数：6

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