2qzd: Difference between revisions
New page: left|200px<br /> <applet load="2qzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qzd" /> '''Fitted structure of SCR4 of DAF into cryoEM... |
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'''Fitted structure of SCR4 of DAF into cryoEM density'''<br /> | '''Fitted structure of SCR4 of DAF into cryoEM density'''<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== | ||
2QZD 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:// | 2QZD 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=2QZD 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 11:50:04 2008'' | ||
Revision as of 12:50, 23 January 2008
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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.
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Single protein
- Bowman, V.D.
- Chipman, P.R.
- Hafenstein, S.
- Kelly, C.M.Bator.
- Lin, F.
- Medof, M.E.
- Rossmann, M.G.
- Alternative splicing
- Blood group antigen
- Complement pathway
- Glycoprotein
- Gpi-anchor
- Immune response
- Immune system
- Innate immunity
- Lipoprotein
- Membrane
- Polymorphism
- Scr4 of daf from 1ojv fitted into cryoem density
- Sushi