登革热病毒和西尼罗河病毒黄病毒属NS3蛋白酶激活的结构基础

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

作者信息

Erbel Paul, Schiering Nikolaus, D'Arcy Allan, Renatus Martin, Kroemer Markus, Lim Siew Pheng, Yin Zheng, Keller Thomas H, Vasudevan Subhash G, Hommel Ulrich

机构信息

Novartis Institutes for Biomedical Research, Protease Platform, 4002 Basel, Switzerland.

出版信息

Nat Struct Mol Biol. 2006 Apr;13(4):372-3. doi: 10.1038/nsmb1073. Epub 2006 Mar 12.

DOI:10.1038/nsmb1073

PMID:16532006

Abstract

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.

摘要

黄病毒的复制需要病毒NS3蛋白酶（NS3pro）对其多聚蛋白进行正确加工。NS2B的一个47个残基的区域对于NS3pro的激活至关重要。在此，我们报告了登革热NS2B-NS3pro复合物和西尼罗河病毒NS2B-NS3pro复合物与一种基于底物的抑制剂的晶体结构。这些结构确定了NS3pro底物识别的关键残基，并阐明了NS3pro的激活机制。