1nn8: Difference between revisions
New page: left|200px<br /> <applet load="1nn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nn8" /> '''CryoEM structure of poliovirus receptor bou... |
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[[Image:1nn8.gif|left|200px]]<br /> | [[Image:1nn8.gif|left|200px]]<br /><applet load="1nn8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''CryoEM structure of poliovirus receptor bound to poliovirus'''<br /> | '''CryoEM structure of poliovirus receptor bound to poliovirus'''<br /> | ||
==Overview== | ==Overview== | ||
Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) | Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry. Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface. The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155. The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating. In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating. The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization. Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1NN8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1NN8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NN8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bator, C | [[Category: Bator, C M.]] | ||
[[Category: Bowman, V | [[Category: Bowman, V D.]] | ||
[[Category: Chipman, P | [[Category: Chipman, P R.]] | ||
[[Category: He, Y.]] | [[Category: He, Y.]] | ||
[[Category: Kuhn, R | [[Category: Kuhn, R J.]] | ||
[[Category: Mueller, S.]] | [[Category: Mueller, S.]] | ||
[[Category: Mukhopadhyay, S.]] | [[Category: Mukhopadhyay, S.]] | ||
[[Category: Peng, X.]] | [[Category: Peng, X.]] | ||
[[Category: Rossmann, M | [[Category: Rossmann, M G.]] | ||
[[Category: Wimmer, E.]] | [[Category: Wimmer, E.]] | ||
[[Category: MYR]] | [[Category: MYR]] | ||
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[[Category: picornavirus]] | [[Category: picornavirus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:55 2008'' | ||
Revision as of 15:07, 21 February 2008
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CryoEM structure of poliovirus receptor bound to poliovirus
OverviewOverview
Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry. Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface. The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155. The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating. In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating. The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization. Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
DiseaseDisease
Known diseases associated with this structure: Polio, susceptibility to OMIM:[173850]
About this StructureAbout this Structure
1NN8 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Complexes of poliovirus serotypes with their common cellular receptor, CD155., He Y, Mueller S, Chipman PR, Bator CM, Peng X, Bowman VD, Mukhopadhyay S, Wimmer E, Kuhn RJ, Rossmann MG, J Virol. 2003 Apr;77(8):4827-35. PMID:12663789
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