2QZH

SCR2/3 of DAF from the NMR structure 1nwv fitted into a cryoEM reconstruction of CVB3-RD complexed with DAF

2QZH の概要

• エントリーDOI: 10.2210/pdb2qzh/pdb
• EMDBエントリー: 1412
• 分子名称: Complement decay-accelerating factor (1 entity in total)
• 機能のキーワード: scr2-3 of daf fitted into cryoem density of cvb3-rd complexed with daf, alternative splicing, blood group antigen, complement pathway, glycoprotein, gpi-anchor, immune response, innate immunity, lipoprotein, membrane, polymorphism, sushi, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14351.30

構造登録者

Hafenstein, S.,Bowman, V.D.,Chipman, P.R.,Bator Kelly, C.M.,Lin, F.,Medof, M.E.,Rossmann, M.G. (登録日: 2007-08-16, 公開日: 2007-10-30, 最終更新日: 2024-02-21)

主引用文献

Hafenstein, S.,Bowman, V.D.,Chipman, P.R.,Kelly, C.M.,Lin, F.,Medof, M.E.,Rossmann, M.G.
Interaction of decay-accelerating factor with coxsackievirus b3.
J.Virol., 81:12927-12935, 2007

PubMed Abstract: Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes.

PubMed: 17804498
DOI: 10.1128/JVI.00931-07

実験手法

ELECTRON MICROSCOPY (14 Å)