Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.,Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM. Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution. Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219
