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分辨率为2.0埃的鼠白血病病毒受体结合糖蛋白结构

Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.

作者信息

Fass D, Davey R A, Hamson C A, Kim P S, Cunningham J M, Berger J M

机构信息

Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.

出版信息

Science. 1997 Sep 12;277(5332):1662-6. doi: 10.1126/science.277.5332.1662.

Abstract

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.

摘要

逆转录病毒感染的一个关键步骤是病毒与靶细胞上的受体结合。通过X射线晶体学确定了弗氏小鼠白血病病毒包膜糖蛋白受体结合结构域的结构,分辨率达到2.0埃。该结构域的核心是一个反平行β折叠三明治结构,两条链间的环在三明治顶部形成一个螺旋亚结构域。在具有不同嗜性的哺乳动物C型逆转录病毒中,螺旋区域而非β折叠三明治区域的残基具有高度变异性,这表明螺旋亚结构域决定了病毒的受体特异性。

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