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''' | + | {{Structure |
| + | |PDB= 1al2 |SIZE=350|CAPTION= <scene name='initialview01'>1al2</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 V1160I''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AL2 is a [ | + | 1AL2 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=1AL2 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 09:59:04 2008'' |
Revision as of 07:59, 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 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 Thu Mar 20 09:59:04 2008
