1al2
From Proteopedia
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|PDB= 1al2 |SIZE=350|CAPTION= <scene name='initialview01'>1al2</scene>, resolution 2.9Å | |PDB= 1al2 |SIZE=350|CAPTION= <scene name='initialview01'>1al2</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> | + | |LIGAND= <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SPH:SPHINGOSINE'>SPH</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1al2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al2 OCA], [http://www.ebi.ac.uk/pdbsum/1al2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1al2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hogle, J M.]] | [[Category: Hogle, J M.]] | ||
[[Category: Wien, M W.]] | [[Category: Wien, M W.]] | ||
| - | [[Category: MYR]] | ||
| - | [[Category: SPH]] | ||
[[Category: coat protein]] | [[Category: coat protein]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
| Line 33: | Line 34: | ||
[[Category: poliovirus]] | [[Category: poliovirus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:31 2008'' |
Revision as of 15:42, 30 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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