Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution
Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution
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DOI：
10.1126/science.277.5332.1662
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发表时间：
1997-09-12
期刊：
影响因子：
56.9
通讯作者：
Berger, JM
中科院分区：
文献类型：
--
作者：
Fass, D;Davey, RA;Berger, JM
逆转录病毒感染的一个重要步骤是病毒与靶细胞上的受体结合。通过X射线晶体学测定Friend鼠白血病病毒包膜糖蛋白的受体结合结构域的结构，分辨率为2.0埃。该结构域的核心是一个反平行的β夹心结构，两个链间环在夹心结构的顶部形成一个螺旋亚结构域。在哺乳动物C型逆转录病毒中，螺旋区域中的残基高度可变，但β夹心结构中的残基则没有，具有不同的向性，这表明螺旋亚结构域决定了病毒的受体特异性。
An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich, The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.