1ar9: Difference between revisions
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[[Image:1ar9.gif|left|200px]] | [[Image:1ar9.gif|left|200px]] | ||
'''P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y''' | {{Structure | ||
|PDB= 1ar9 |SIZE=350|CAPTION= <scene name='initialview01'>1ar9</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> and <scene name='pdbligand=SPH:SPHINGOSINE'>SPH</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AR9 is a [ | 1AR9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AR9 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9253417 9253417] | ||
[[Category: Human poliovirus 1]] | [[Category: Human poliovirus 1]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: poliovirus]] | [[Category: poliovirus]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:20 2008'' | ||
Revision as of 11:01, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y
OverviewOverview
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 StructureAbout this Structure
1AR9 is a Protein complex structure of sequences from Human poliovirus 1. Full crystallographic information is available from OCA.
ReferenceReference
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
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