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1LCS

RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS

Summary for 1LCS
Entry DOI10.2210/pdb1lcs/pdb
Related1AOL
DescriptorFELINE 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 Keywordsantiparallel beta-sandwich glycoprotein, viral protein
Biological sourceFeline leukemia virus
Total number of polymer chains2
Total formula weight49209.59
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 citationBarnett, 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: 12552012
DOI: 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

237735

数据于2025-06-18公开中

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