Botos I, Wlodawer A
National Cancer Institute, MCL, Bldg. 536, Rm. 5, Frederick, Maryland 21702-1201, USA.
Cell Mol Life Sci. 2003 Feb;60(2):277-87. doi: 10.1007/s000180300023.
Cyanovirin-N (CV-N), an 11-kDa protein from the cyanobacterium Nostoc ellipsosporum, is a highly potent virucidal agent that has generated interest as a lead natural product for the prevention and chemotherapy of human immunodeficiency virus infection. The antiviral activity of CV-N is mediated through specific, high-affinity interactions with the viral surface envelope glycoproteins. A number of structures of wild-type, mutant and sequence-shuffled CV-N have been solved by nuclear magnetic resonance and crystallography, showing that the protein exists as either a quasi-symmetric two-domain monomer or a domain-swapped dimer. Structures of several complexes of CV-N with oligosaccharides help in explaining the unique mode of high-affinity binding of these molecules to both forms of CV-N.
蓝藻素-N(CV-N)是一种来自椭圆念珠藻的11千道尔顿蛋白质,是一种高效的杀病毒剂,作为预防和化疗人类免疫缺陷病毒感染的先导天然产物引起了人们的关注。CV-N的抗病毒活性是通过与病毒表面包膜糖蛋白的特异性、高亲和力相互作用介导的。通过核磁共振和晶体学解析了野生型、突变型和序列改组的CV-N的多种结构,表明该蛋白质以准对称的双结构域单体或结构域交换二聚体形式存在。CV-N与寡糖的几种复合物的结构有助于解释这些分子与两种形式的CV-N高亲和力结合的独特模式。