STRUCTURE OF INFLUENZA HEMAGGLUTININ AT THE PH OF MEMBRANE-FUSION

被引：1373

作者：

BULLOUGH, PA

HUGHSON, FM

SKEHEL, JJ

WILEY, DC

机构：

[1] HARVARD UNIV,DEPT BIOCHEM & MOLEC BIOL,CAMBRIDGE,MA 02138

[2] HARVARD UNIV,HOWARD HUGHES MED INST,CAMBRIDGE,MA 02138

[3] NATL INST MED RES,LONDON NW7 1AA,ENGLAND

来源：

NATURE | 1994年 / 371卷 / 6492期

关键词：

D O I：

10.1038/371037a0

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：

Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 Angstrom to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.

引用

页码：37 / 43

页数：7

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