2NSU

Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex

2NSU の概要

• エントリーDOI: 10.2210/pdb2nsu/pdb
• 関連するPDBエントリー: 1CX8
• EMDBエントリー: 1288
• 分子名称: Transferrin receptor protein 1 (1 entity in total)
• 機能のキーワード: transferrin receptor, virus-receptor complex, metal transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 143245.92

構造登録者

Hafenstein, S.,Kostyuchenko, V.A.,Rossmann, M.G. (登録日: 2006-11-06, 公開日: 2007-03-27, 最終更新日: 2024-11-13)

主引用文献

Hafenstein, S.,Palermo, L.M.,Kostyuchenko, V.A.,Xiao, C.,Morais, M.C.,Nelson, C.D.,Bowman, V.D.,Battisti, A.J.,Chipman, P.R.,Parrish, C.R.,Rossmann, M.G.
Asymmetric binding of transferrin receptor to parvovirus capsids.
Proc.Natl.Acad.Sci.Usa, 104:6585-6589, 2007

PubMed Abstract: Although many viruses are icosahedral when they initially bind to one or more receptor molecules on the cell surface, such an interaction is asymmetric, probably causing a breakdown in the symmetry and conformation of the original infecting virion in preparation for membrane penetration and release of the viral genome. Cryoelectron microscopy and biochemical analyses show that transferrin receptor, the cellular receptor for canine parvovirus, can bind to only one or a few of the 60 icosahedrally equivalent sites on the virion, indicating that either canine parvovirus has inherent asymmetry or binding of receptor induces asymmetry. The asymmetry of receptor binding to canine parvovirus is reminiscent of the special portal in tailed bacteriophages and some large, icosahedral viruses. Asymmetric interactions of icosahedral viruses with their hosts might be a more common phenomenon than previously thought and may have been obscured by averaging in previous crystallographic and electron microscopic structure determinations.

PubMed: 17420467
DOI: 10.1073/pnas.0701574104

実験手法

ELECTRON MICROSCOPY (27 Å)