1al2
From Proteopedia
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[[Image:1al2.gif|left|200px]] | [[Image:1al2.gif|left|200px]] | ||
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'''P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT V1160I''' | '''P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT V1160I''' | ||
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[[Category: Hogle, J M.]] | [[Category: Hogle, J M.]] | ||
[[Category: Wien, M W.]] | [[Category: Wien, M W.]] | ||
| - | [[Category: | + | [[Category: Coat protein]] |
| - | [[Category: | + | [[Category: Icosahedral virus]] |
| - | [[Category: | + | [[Category: Picornavirus]] |
| - | [[Category: | + | [[Category: Poliovirus]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:24:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:24, 2 May 2008
P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT V1160I
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
1AL2 is a Protein complex structure of sequences from Human poliovirus 1. 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 Fri May 2 10:24:31 2008
