Bornholdt Zachary A, Prasad B V Venkataram
Department of Molecular Virology and Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Nat Struct Mol Biol. 2006 Jun;13(6):559-60. doi: 10.1038/nsmb1099. Epub 2006 May 21.
The nonstructural protein NS1 of influenza virus is an antagonist of host immune responses and is implicated in virulence. It has two domains, an N-terminal double-stranded RNA-binding domain (RBD) and an effector domain crucial for RBD function, for nuclear export and for sequestering messenger RNA-processing proteins. Here we present the crystallographic structure of the effector domain, which has a novel fold and suggests mechanisms for increased virulence in H5N1 strains.
流感病毒的非结构蛋白NS1是宿主免疫反应的拮抗剂，并与病毒毒力有关。它有两个结构域，一个N端双链RNA结合结构域（RBD）和一个对RBD功能、核输出以及隔离信使RNA加工蛋白至关重要的效应结构域。在此，我们展示了效应结构域的晶体结构，其具有新颖的折叠方式，并揭示了H5N1毒株毒力增强的机制。
