Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.
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.
Fass
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Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
Davey
R A
RA
Hamson
C A
CA
Kim
P S
PS
Cunningham
J M
JM
Berger
J M
JM
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism; D018360:Crystallography, X-Ray; D005622:Friend murine leukemia virus / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011991:Receptors, Virus / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism
D002352:Carrier Proteins; C108061:Fr-RBD protein, Friend murine leukemia virus; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; C070506:ecotropic murine leukemia virus receptor