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Science 12 September 1997:
Vol. 277. no. 5332, pp. 1662 - 1666
DOI: 10.1126/science.277.5332.1662
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Reports

Structure of a Murine Leukemia Virus Receptor-Binding Glycoprotein at 2.0 Angstrom Resolution

Deborah Fass, Robert A. Davey, Christian A. Hamson, Peter S. Kim, * James M. Cunningham, * James M. Berger

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.

D. Fass and P. S. Kim, Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
R. A. Davey, C. A. Hamson, J. M. Cunningham, Howard Hughes Medical Institute, Division of Hematology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Room 30, Thorn Building, 20 Shattuck Street, Boston, MA 02115, USA.
J. M. Berger, Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
*   To whom correspondence should be addressed.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)