2qzf: Difference between revisions

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[[Image:2qzf.gif|left|200px]]
{{Seed}}
[[Image:2qzf.png|left|200px]]


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{{STRUCTURE_2qzf|  PDB=2qzf  |  SCENE=  }}  
{{STRUCTURE_2qzf|  PDB=2qzf  |  SCENE=  }}  


'''SCR1 of DAF from 1ojv fitted into cryoEM density'''
===SCR1 of DAF from 1ojv fitted into cryoEM density===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_17804498}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17804498 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17804498}}


==About this Structure==
==About this Structure==
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[[Category: Scr1 of daf from structure 1ojv fitted into cryoem density]]
[[Category: Scr1 of daf from structure 1ojv fitted into cryoem density]]
[[Category: Sushi]]
[[Category: Sushi]]
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