1aol | pdb_00001aol

FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN

spinqualitylabelsall models 1aol, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aol is a 1 chain structure with sequence from Friend murine leukemia virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, ZN Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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