1piv
From Proteopedia
(New page: 200px<br /><applet load="1piv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1piv, resolution 2.9Å" /> '''BINDING OF THE ANTIVI...) |
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| - | [[Image:1piv.gif|left|200px]]<br /><applet load="1piv" size=" | + | [[Image:1piv.gif|left|200px]]<br /><applet load="1piv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1piv, resolution 2.9Å" /> | caption="1piv, resolution 2.9Å" /> | ||
'''BINDING OF THE ANTIVIRAL DRUG WIN51711 TO THE SABIN STRAIN OF TYPE 3 POLIOVIRUS: STRUCTURAL COMPARISON WITH DRUG BINDING IN RHINOVIRUS 14'''<br /> | '''BINDING OF THE ANTIVIRAL DRUG WIN51711 TO THE SABIN STRAIN OF TYPE 3 POLIOVIRUS: STRUCTURAL COMPARISON WITH DRUG BINDING IN RHINOVIRUS 14'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the Sabin strain of type 3 poliovirus (P3/Sabin) | + | The crystal structure of the Sabin strain of type 3 poliovirus (P3/Sabin) complexed with the antiviral drug WIN51711 has been determined at 2.9 A resolution. Drugs of this kind are known to inhibit the uncoating of the virus during infection, by stabilizing the capsid against receptor-induced conformational changes. The electron density for the bound drug is very well defined so that its position and orientation are unambiguous. The drug binds in a nearly extended conformation, slightly bent in the middle, in a blind pocket formed predominantly by hydrophobic residues in the core of the beta-barrel of capsid protein VP1. Comparisons between this structure, the corresponding drug complex in human rhinovirus 14 (HRV 14), and the native structures of both viruses demonstrate that the binding of WIN51711 has markedly different effects on the structures of these two viruses. Unlike HRV14, wherein large conformational changes are observed in the coat protein after drug binding, the binding of this drug in poliovirus does not induce any significant conformational changes in the structure of the capsid protein, though the drug has a greater inhibitory effect in P3/Sabin than in HRV14. The implications of this result for the mechanism of capsid stabilization are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1PIV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Viruses Viruses] with MYR and W71 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PIV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Viruses Viruses] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=W71:'>W71</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Viruses]] | [[Category: Viruses]] | ||
| - | [[Category: Filman, D | + | [[Category: Filman, D J.]] |
| - | [[Category: Grant, R | + | [[Category: Grant, R A.]] |
| - | [[Category: Hiremath, C | + | [[Category: Hiremath, C N.]] |
| - | [[Category: Hogle, J | + | [[Category: Hogle, J M.]] |
[[Category: MYR]] | [[Category: MYR]] | ||
[[Category: W71]] | [[Category: W71]] | ||
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[[Category: virus]] | [[Category: virus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:15 2008'' |
Revision as of 12:29, 21 February 2008
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BINDING OF THE ANTIVIRAL DRUG WIN51711 TO THE SABIN STRAIN OF TYPE 3 POLIOVIRUS: STRUCTURAL COMPARISON WITH DRUG BINDING IN RHINOVIRUS 14
Overview
The crystal structure of the Sabin strain of type 3 poliovirus (P3/Sabin) complexed with the antiviral drug WIN51711 has been determined at 2.9 A resolution. Drugs of this kind are known to inhibit the uncoating of the virus during infection, by stabilizing the capsid against receptor-induced conformational changes. The electron density for the bound drug is very well defined so that its position and orientation are unambiguous. The drug binds in a nearly extended conformation, slightly bent in the middle, in a blind pocket formed predominantly by hydrophobic residues in the core of the beta-barrel of capsid protein VP1. Comparisons between this structure, the corresponding drug complex in human rhinovirus 14 (HRV 14), and the native structures of both viruses demonstrate that the binding of WIN51711 has markedly different effects on the structures of these two viruses. Unlike HRV14, wherein large conformational changes are observed in the coat protein after drug binding, the binding of this drug in poliovirus does not induce any significant conformational changes in the structure of the capsid protein, though the drug has a greater inhibitory effect in P3/Sabin than in HRV14. The implications of this result for the mechanism of capsid stabilization are discussed.
About this Structure
1PIV is a Protein complex structure of sequences from Viruses with and as ligands. Full crystallographic information is available from OCA.
Reference
Binding of the antiviral drug WIN51711 to the sabin strain of type 3 poliovirus: structural comparison with drug binding in rhinovirus 14., Hiremath CN, Grant RA, Filman DJ, Hogle JM, Acta Crystallogr D Biol Crystallogr. 1995 Jul 1;51(Pt 4):473-89. PMID:15299834
Page seeded by OCA on Thu Feb 21 14:29:15 2008
Categories: Protein complex | Viruses | Filman, D J. | Grant, R A. | Hiremath, C N. | Hogle, J M. | MYR | W71 | Icosahedral virus | Virus
