1LCS
RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS
Summary for 1LCS
Entry DOI | 10.2210/pdb1lcs/pdb |
Related | 1AOL |
Descriptor | FELINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-2)-beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | antiparallel beta-sandwich glycoprotein, viral protein |
Biological source | Feline leukemia virus |
Total number of polymer chains | 2 |
Total formula weight | 49209.59 |
Authors | Barnett, A.L.,Wensel, D.L.,Li, W.,Fass, D.,Cunningham, J.M. (deposition date: 2002-04-06, release date: 2003-04-08, Last modification date: 2024-11-13) |
Primary citation | Barnett, A.L.,Wensel, D.L.,Li, W.,Fass, D.,Cunningham, J.M. Structure and Mechanism of a Coreceptor for Infection by a pathogenic feline retrovirus J.Virol., 77:2717-2729, 2003 Cited by PubMed Abstract: Infection of T lymphocytes by the cytopathic retrovirus feline leukemia virus subgroup T (FeLV-T) requires FeLIX, a cellular coreceptor that is encoded by an endogenous provirus and closely resembles the receptor-binding domain (RBD) of feline leukemia virus subgroup B (FeLV-B). We determined the structure of FeLV-B RBD, which has FeLIX activity, to a 2.5-A resolution by X-ray crystallography. The structure of the receptor-specific subdomain of this glycoprotein differs dramatically from that of Friend murine leukemia virus (Fr-MLV), which binds a different cell surface receptor. Remarkably, we find that Fr-MLV RBD also activates FeLV-T infection of cells expressing the Fr-MLV receptor and that FeLV-B RBD is a competitive inhibitor of infection under these conditions. These studies suggest that FeLV-T infection relies on the following property of mammalian leukemia virus RBDs: the ability to couple interaction with one of a variety of receptors to the activation of a conserved membrane fusion mechanism. A comparison of the FeLV-B and Fr-MLV RBD structures illustrates how receptor-specific regions are linked to conserved elements critical for postbinding events in virus entry. PubMed: 12552012DOI: 10.1128/JVI.77.4.2717-2729.2003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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