1LCS

RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS

1LCS の概要

• エントリーDOI: 10.2210/pdb1lcs/pdb
• 関連するPDBエントリー: 1AOL
• 分子名称: 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)
• 機能のキーワード: antiparallel beta-sandwich glycoprotein, viral protein
• 由来する生物種: Feline leukemia virus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49209.59

構造登録者

Barnett, A.L.,Wensel, D.L.,Li, W.,Fass, D.,Cunningham, J.M. (登録日: 2002-04-06, 公開日: 2003-04-08, 最終更新日: 2024-11-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.5 Å)