1DGI

Cryo-EM structure of human poliovirus(serotype 1)complexed with three domain CD155

1DGI の概要

• エントリーDOI: 10.2210/pdb1dgi/pdb
• 関連するPDBエントリー: 1BIH 1CIC 1NEU 2PLV
• 分子名称: POLIOVIRUS RECEPTOR, VP1, VP2, ... (5 entities in total)
• 機能のキーワード: cd155, pvr, human poliovirus, poliovirus-receptor complex, icosahedral virus, virus-receptor complex, virus/receptor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 127686.07

構造登録者

He, Y.,Bowman, V.D.,Mueller, S.,Bator, C.M.,Bella, J.,Peng, X.,Baker, T.S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G. (登録日: 1999-11-24, 公開日: 2000-01-24, 最終更新日: 2024-02-07)

主引用文献

He, Y.,Bowman, V.D.,Mueller, S.,Bator, C.M.,Bella, J.,Peng, X.,Baker, T.S.,Wimmer, E.,Kuhn, R.J.,Rossmann, M.G.
Interaction of the poliovirus receptor with poliovirus.
Proc.Natl.Acad.Sci.USA, 97:79-84, 2000

PubMed Abstract: The structure of the extracellular, three-domain poliovirus receptor (CD155) complexed with poliovirus (serotype 1) has been determined to 22-A resolution by means of cryo-electron microscopy and three-dimensional image-reconstruction techniques. Density corresponding to the receptor was isolated in a difference electron density map and fitted with known structures, homologous to those of the three individual CD155 Ig-like domains. The fit was confirmed by the location of carbohydrate moieties in the CD155 glycoprotein, the conserved properties of elbow angles in the structures of cell surface molecules with Ig-like folds, and the concordance with prior results of CD155 and poliovirus mutagenesis. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. However, the orientation of the long, slender CD155 molecule relative to the poliovirus surface is quite different from the orientation of intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues that provide specificity of recognition differ for the two receptors. The principal feature of receptor binding common to these two picornaviruses is the site in the canyon at which binding occurs. This site may be a trigger for initiation of the subsequent uncoating step required for viral infection.

PubMed: 10618374
DOI: 10.1073/pnas.97.1.79

実験手法

ELECTRON MICROSCOPY (22 Å)