2qzh: Difference between revisions
New page: left|200px<br /> <applet load="2qzh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qzh" /> '''SCR2/3 of DAF from the NMR structure 1nwv f... |
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[[Image:2qzh.gif|left|200px]]<br /> | [[Image:2qzh.gif|left|200px]]<br /><applet load="2qzh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''SCR2/3 of DAF from the NMR structure 1nwv fitted into a cryoEM reconstruction of CVB3-RD complexed with DAF'''<br /> | '''SCR2/3 of DAF from the NMR structure 1nwv fitted into a cryoEM reconstruction of CVB3-RD complexed with DAF'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
2QZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2QZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kelly, C.M.Bator.]] | [[Category: Kelly, C.M.Bator.]] | ||
[[Category: Lin, F.]] | [[Category: Lin, F.]] | ||
[[Category: Medof, | [[Category: Medof, M.E.]] | ||
[[Category: Rossmann, M.G.]] | [[Category: Rossmann, M.G.]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
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[[Category: sushi]] | [[Category: sushi]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:50:09 2008'' | ||
