1ar7

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(New page: 200px<br /><applet load="1ar7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ar7, resolution 2.9&Aring;" /> '''P1/MAHONEY POLIOVIRUS...)
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[[Image:1ar7.gif|left|200px]]<br /><applet load="1ar7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ar7.gif|left|200px]]<br /><applet load="1ar7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ar7, resolution 2.9&Aring;" />
caption="1ar7, resolution 2.9&Aring;" />
'''P1/MAHONEY POLIOVIRUS, DOUBLE MUTANT P1095S + H2142Y'''<br />
'''P1/MAHONEY POLIOVIRUS, DOUBLE MUTANT P1095S + H2142Y'''<br />
==Overview==
==Overview==
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In order to better understand the process of cell entry for non-enveloped, viruses, we have solved the crystal structures of five poliovirus mutants, which can infect cells expressing mutant poliovirus receptors. Four of, these structures have been solved from frozen crystals using, cryocrystallographic data collection methods. The mutations have a range, of structural consequences, from small local perturbations to significant, loop rearrangements. All of the mutant viruses are more labile to, conversion to an apparent cell entry intermediate, suggesting that these, mutant viruses could compensate for the suboptimal receptors by lowering, the thermal energy required to undergo the receptor-mediated, conformational change.
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In order to better understand the process of cell entry for non-enveloped viruses, we have solved the crystal structures of five poliovirus mutants which can infect cells expressing mutant poliovirus receptors. Four of these structures have been solved from frozen crystals using cryocrystallographic data collection methods. The mutations have a range of structural consequences, from small local perturbations to significant loop rearrangements. All of the mutant viruses are more labile to conversion to an apparent cell entry intermediate, suggesting that these mutant viruses could compensate for the suboptimal receptors by lowering the thermal energy required to undergo the receptor-mediated conformational change.
==About this Structure==
==About this Structure==
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1AR7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with MYR and SPH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AR7 OCA].
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1AR7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=SPH:'>SPH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AR7 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Curry, S.]]
[[Category: Curry, S.]]
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[[Category: Filman, D.J.]]
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[[Category: Filman, D J.]]
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[[Category: Hogle, J.M.]]
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[[Category: Hogle, J M.]]
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[[Category: Wien, M.W.]]
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[[Category: Wien, M W.]]
[[Category: MYR]]
[[Category: MYR]]
[[Category: SPH]]
[[Category: SPH]]
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[[Category: poliovirus]]
[[Category: poliovirus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:03:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:25 2008''

Revision as of 09:47, 21 February 2008


1ar7, resolution 2.9Å

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P1/MAHONEY POLIOVIRUS, DOUBLE MUTANT P1095S + H2142Y

Overview

In order to better understand the process of cell entry for non-enveloped viruses, we have solved the crystal structures of five poliovirus mutants which can infect cells expressing mutant poliovirus receptors. Four of these structures have been solved from frozen crystals using cryocrystallographic data collection methods. The mutations have a range of structural consequences, from small local perturbations to significant loop rearrangements. All of the mutant viruses are more labile to conversion to an apparent cell entry intermediate, suggesting that these mutant viruses could compensate for the suboptimal receptors by lowering the thermal energy required to undergo the receptor-mediated conformational change.

About this Structure

1AR7 is a Protein complex structure of sequences from Human poliovirus 1 with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural studies of poliovirus mutants that overcome receptor defects., Wien MW, Curry S, Filman DJ, Hogle JM, Nat Struct Biol. 1997 Aug;4(8):666-74. PMID:9253417

Page seeded by OCA on Thu Feb 21 11:47:25 2008

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