2qzf

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spinqualitylabelsall models PDB ID 2qzf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
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SCR1 of DAF from 1ojv fitted into cryoEM density

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

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 Structure

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

Reference

Interaction of decay-accelerating factor with coxsackievirus B3., Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG, J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:17804498

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