3URO

Poliovirus receptor CD155 D1D2

「3EOW」から置き換えられました

3URO の概要

• エントリーDOI: 10.2210/pdb3uro/pdb
• 関連するPDBエントリー: 3EPC 3EPD 3EPF
• 分子名称: Poliovirus receptor (1 entity in total)
• 機能のキーワード: poliovirus receptor ectodomain, immunoglobulin super family, cell adhesion, cell membrane, glycoprotein, host-virus interaction, immunoglobulin domain, membrane, receptor, secreted, transmembrane, viral protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform Alpha: Cell membrane; Single-pass type I membrane protein. Isoform Delta: Cell membrane; Single-pass type I membrane protein. Isoform Beta: Secreted. Isoform Gamma: Secreted: P15151
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24355.65

構造登録者

Zhang, P.,Mueller, S.,Morais, M.C.,Bator, C.M.,Bowman, V.D.,Hafenstein, S.,Wimmer, E.,Rossmann, M.G. (登録日: 2011-11-22, 公開日: 2011-12-07, 最終更新日: 2024-11-06)

主引用文献

Zhang, P.,Mueller, S.,Morais, M.C.,Bator, C.M.,Bowman, V.D.,Hafenstein, S.,Wimmer, E.,Rossmann, M.G.
Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.
Proc.Natl.Acad.Sci.USA, 105:18284-18289, 2008

PubMed Abstract: When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-A resolution and fitted into approximately 8.5-A resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell.

PubMed: 19011098
DOI: 10.1073/pnas.0807848105

実験手法

X-RAY DIFFRACTION (3.5005 Å)