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.