1AOL
FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN
Summary for 1AOL
| Entry DOI | 10.2210/pdb1aol/pdb |
| Descriptor | GP70, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (4 entities in total) |
| Functional Keywords | coat protein, viral glycoprotein, retrovirus, viral protein |
| Biological source | Friend murine leukemia virus |
| Cellular location | Transmembrane protein: Virion membrane; Single-pass type I membrane protein (By similarity). Surface protein: Virion membrane; Peripheral membrane protein. R-peptide: Host cell membrane; Peripheral membrane protein (By similarity): P03390 |
| Total number of polymer chains | 1 |
| Total formula weight | 26036.00 |
| Authors | Fass, D.,Davey, R.A.,Hamson, C.A.,Kim, P.S.,Cunningham, J.M.,Berger, J.M. (deposition date: 1997-07-08, release date: 1997-10-15, Last modification date: 2020-07-29) |
| Primary citation | Fass, D.,Davey, R.A.,Hamson, C.A.,Kim, P.S.,Cunningham, J.M.,Berger, J.M. Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution. Science, 277:1662-1666, 1997 Cited by PubMed Abstract: 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. PubMed: 9287219DOI: 10.1126/science.277.5332.1662 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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