STRUCTURE OF A MURINE LEUKEMIA-VIRUS RECEPTOR-BINDING GLYCOPROTEIN AT2.0 ANGSTROM RESOLUTION

Citation
D. Fass et al., STRUCTURE OF A MURINE LEUKEMIA-VIRUS RECEPTOR-BINDING GLYCOPROTEIN AT2.0 ANGSTROM RESOLUTION, Science, 277(5332), 1997, pp. 1662-1666
Citations number
37
Categorie Soggetti
Multidisciplinary Sciences
Journal title
ISSN journal
00368075
Volume
277
Issue
5332
Year of publication
1997
Pages
1662 - 1666
Database
ISI
SICI code
0036-8075(1997)277:5332<1662:SOAMLR>2.0.ZU;2-L
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-bindin g domain of the envelope glycoprotein from Friend murine leukemia viru s was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two inte rstrand loops forming a helical subdomain atop the sandwich, The resid ues in the helical region, but not in the beta sandwich, are highly va riable among mammalian C-type retroviruses with distinct tropisms, ind icating that the helical subdomain determines the receptor specificity of the virus.