2QZD

Fitted structure of SCR4 of DAF into cryoEM density

Summary for 2QZD

• Entry DOI: 10.2210/pdb2qzd/pdb
• EMDB information: 1412
• Descriptor: Complement decay-accelerating factor (1 entity in total)
• Functional Keywords: scr4 of daf from 1ojv fitted into cryoem density, blood group antigen, complement pathway, glycoprotein, gpi-anchor, immune response, innate immunity, lipoprotein, membrane, sushi, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 7274.99

Authors

Hafenstein, S.,Bowman, V.D.,Chipman, P.R.,Bator Kelly, C.M.,Lin, F.,Medof, M.E.,Rossmann, M.G. (deposition date: 2007-08-16, release date: 2007-10-30, Last modification date: 2024-10-16)

Primary citation

Hafenstein, S.,Bowman, V.D.,Chipman, P.R.,Bator 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

Experimental method

ELECTRON MICROSCOPY (14 Å)