1P5W

The structures of host range controlling regions of the capsids of canine and feline parvoviruses and mutants

1P5W の概要

• エントリーDOI: 10.2210/pdb1p5w/pdb
• 関連するPDBエントリー: 1P5Y
• 分子名称: 5'-D(P*(3DR)P*TP*AP*CP*CP*TP*CP*TP*TP*GP*C)-3', Coat protein VP2, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: parvovirade, canine parvovirus, icosahedral virus, virus-dna complex, virus/dna
• 由来する生物種: Canine parvovirus
• 細胞内の位置: Virion: P17455
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64853.72

構造登録者

Agbandje-McKenna, M.,Govindasamy, L. (登録日: 2003-04-28, 公開日: 2003-08-26, 最終更新日: 2024-11-06)

主引用文献

Govindasamy, L.,Hueffer, K.,Parrish, C.R.,Agbandje-McKenna, M.
Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants.
J.Virol., 77:12211-12221, 2003

PubMed Abstract: Canine parvovirus (CPV) and feline panleukopenia virus (FPV) differ in their ability to infect dogs and dog cells. Canine cell infection is a specific property of CPV and depends on the ability of the virus to bind the canine transferrin receptor (TfR), as well as other unidentified factors. Three regions in the capsid structure, located around VP2 residues 93, 300, and 323, can all influence canine TfR binding and canine cell infection. These regions were compared in the CPV and FPV capsid structures that have been determined, as well as in two new structures of CPV capsids that contain substitutions of the VP2 Asn-93 to Asp and Arg, respectively. The new structures, determined by X-ray crystallography to 3.2 and 3.3 A resolutions, respectively, clearly showed differences in the interactions of residue 93 with an adjacent loop on the capsid surface. Each of the three regions show small differences in structure, but each appears to be structurally independent of the others, and the changes likely act together to affect the ability of the capsid to bind the canine TfR and to infect canine cells. This emphasizes the complex nature of capsid alterations that change the virus-cell interaction to allow infection of cells from different hosts.

PubMed: 14581558
DOI: 10.1128/JVI.77.22.12211-12221.2003

実験手法

X-RAY DIFFRACTION (3.3 Å)