THE STRUCTURE OF THE COMPLEX BETWEEN INFLUENZA-VIRUS NEURAMINIDASE AND SIALIC-ACID, THE VIRAL RECEPTOR

被引：354
|
作者：
VARGHESE, JN
MCKIMMBRESCHKIN, JL
CALDWELL, JB
KORTT, AA
COLMAN, PM
机构：
[1] CSIRO, Division of Biomolecular Engineering, Parkville, Victoria
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 1992年 / 14卷 / 03期
关键词：
CRYSTALLOGRAPHIC; NEURAMINIDASE; INFLUENZA VIRUS; SIALIC ACID;
D O I：
10.1002/prot.340140302
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：
Crystallographic studies of neuraminidase-sialic acid complexes indicate that sialic acid is distorted on binding the enzyme. Three arginine residues on the enzyme interact with the carboxylate group of the sugar which is observed to be equatorial to the saccharide ring as a consequence of its distorted geometry. The glycosidic oxygen is positioned within hydrogen-bonding distance of Asp-151, implicating this residue in catalysis.
引用
收藏
页码：327 / 332
页数：6
相关论文
共 50 条
12345