HEPTAD REPEAT SEQUENCES ARE LOCATED ADJACENT TO HYDROPHOBIC REGIONS IN SEVERAL TYPES OF VIRUS FUSION GLYCOPROTEINS
HEPTAD REPEAT SEQUENCES ARE LOCATED ADJACENT TO HYDROPHOBIC REGIONS IN SEVERAL TYPES OF VIRUS FUSION GLYCOPROTEINS
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DOI：
10.1099/0022-1317-71-12-3075
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发表时间：
1990-12-01
影响因子：
3.8
通讯作者：
EASTON, AJ
中科院分区：
文献类型：
--
作者：
CHAMBERS, P;PRINGLE, CR;EASTON, AJ
在副粘病毒融合和逆转录病毒包膜糖蛋白的氨基酸序列中，与α -螺旋盘状螺旋构象一致的七肽重复单元的广泛区域位于疏水、可能与融合相关的区域附近。类似的疏水肽和七肽重复单位的排列存在于冠状病毒聚体蛋白和流感病毒血凝素中。这表明，在病毒进入过程中，这些蛋白质的结构和疏水融合相关区域的功能可能存在相似之处。
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.