Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases

被引：113

作者：

Varghese, JN

Colman, PM

vanDonkelaar, A

Blick, TJ

Sahasrabudhe, A

McKimmBreschkin, JL

机构：

[1] Biomolecular Research Institute, 343 Royal Parade, Parkville

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1997年 / 94卷 / 22期

关键词：

D O I：

10.1073/pnas.94.22.11808

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The x-ray structure of a complex of sialic acid (Neu5Ac) with neuraminidase N9 subtype from A/tern/ AustraIia/G70C/75 influenza virus at 4 degrees C has revealed the location of a second Neu5Ac binding site on the surface of the enzyme, At 18 degrees C, only the enzyme active site contains bound Neu5Ac, Neu5Ac binds in the second site in the chair conformation in a similar way to which it binds to hemagglutinin, The residues that interact with Neu5Ac at this second site are mostly conserved in avian strains, but not in human and swine strains, indicating that it has some as-yet-unknown biological function in birds.

引用

页码：11808 / 11812

页数：5

共 43 条

[1] RED-CELLS BOUND TO INFLUENZA-VIRUS N9 NEURAMINIDASE ARE NOT RELEASED BY THE N9 NEURAMINIDASE ACTIVITY [J].