HEPTAD REPEAT SEQUENCES ARE LOCATED ADJACENT TO HYDROPHOBIC REGIONS IN SEVERAL TYPES OF VIRUS FUSION GLYCOPROTEINS

被引：251

作者：

CHAMBERS, P ^{[1
]}

PRINGLE, CR ^{[1
]}

EASTON, AJ ^{[1
]}

机构：

[1] UNIV WARWICK,DEPT BIOL SCI,COVENTRY CV4 7AL,W MIDLANDS,ENGLAND

来源：

JOURNAL OF GENERAL VIROLOGY | 1990年 / 71卷

关键词：

D O I：

10.1099/0022-1317-71-12-3075

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Extensive regions of heptad repeat units consistent with an alpha-helical coiled coil conformation are located adjacent to hydrophobic, potentially fusion-related regions in the amino acid sequences of paramyxovirus fusion and retrovirus envelope glycoproteins. Similar arrangements of hydrophobic peptides and heptad repeat units exist in coronavirus peplomer proteins and influenza virus haemagglutinins. This suggests that there may be similarities in the structures of these proteins and in the functions of the hydrophobic fusion-related regions during virus entry.

引用

页码：3075 / 3080

页数：6

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