Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus

被引：448

作者：

Erbel, P

Schiering, N

D'Arcy, A

Renatus, M

Kroemer, M

Lim, SP

Yin, Z

Keller, TH

Vasudevan, SG

Hommel, U ^{[1
]}

机构：

[1] Protease Platform, Novartis Inst Biomed Res, CH-4002 Basel, Switzerland

[2] Discovery Technol, Novartis Inst Biomed Res, CH-4002 Basel, Switzerland

[3] Novartis Inst Trop Dis, Singapore 138670, Singapore

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 04期

关键词：

D O I：

10.1038/nsmb1073

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 replication of flaviviruses requires the correct processing of their polyprotein by the viral NS3 protease ( NS3pro). Essential for the activation of NS3pro is a 47-residue region of NS2B. Here we report the crystal structures of a dengue NS2B-NS3pro complex and a West Nile virus NS2B-NS3pro complex with a substrate-based inhibitor. These structures identify key residues for NS3pro substrate recognition and clarify the mechanism of NS3pro activation.

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页码：372 / 373

页数：2

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