2qzd

File:2qzd.gif

spinqualitylabelsall models 2qzd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Fitted structure of SCR4 of DAF into cryoEM density

OverviewOverview

Many entero-, parecho-, and rhinoviruses use IgG-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 IgG-like molecule that binds into the viral canyon, and, decay-accelerating factor (DAF) have been identified as cellular receptors, for coxsackievirus B3 (CVB3). A cryo-electron 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.

DiseaseDisease

Known diseases associated with this structure: Blood group Cromer OMIM:[125240], Blood group, Knops system OMIM:[120620], CR1 deficiency OMIM:[120620], Malaria, severe, resistance to OMIM:[120620], SLE susceptibility OMIM:[120620]

About this StructureAbout this Structure

2QZD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The Interaction of Decay-accelerating Factor with Coxsackievirus B3., Hafenstein S, Bowman VD, Chipman PR, Kelly CM, Lin F, Medof DE, Rossmann MG, J Virol. 2007 Sep 5;. PMID:17804498

Page seeded by OCA on Mon Nov 12 23:35:26 2007