1po1
From Proteopedia
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|PDB= 1po1 |SIZE=350|CAPTION= <scene name='initialview01'>1po1</scene>, resolution 2.9Å | |PDB= 1po1 |SIZE=350|CAPTION= <scene name='initialview01'>1po1</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=J80:(METHYLPYRIDAZINE+PIPERIDINE+BUTYLOXYPHENYL)ETHYLACETATE'>J80</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1po1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1po1 OCA], [http://www.ebi.ac.uk/pdbsum/1po1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1po1 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hiremath, C N.]] | [[Category: Hiremath, C N.]] | ||
[[Category: Hogle, J M.]] | [[Category: Hogle, J M.]] | ||
| - | [[Category: J80]] | ||
| - | [[Category: MYR]] | ||
[[Category: anti-viral drug]] | [[Category: anti-viral drug]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| Line 35: | Line 36: | ||
[[Category: thiol protease]] | [[Category: thiol protease]] | ||
| - | ''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 23:02:16 2008'' |
Revision as of 20:02, 30 March 2008
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| , resolution 2.9Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
POLIOVIRUS (TYPE 1, MAHONEY) IN COMPLEX WITH R80633, AN INHIBITOR OF VIRAL REPLICATION
Overview
Crystal structures of the Mahoney strain of type 1 poliovirus complexed with the antiviral compounds R80633 and R77975 were determined at 2.9 A resolution. These compounds block infection by preventing conformational changes required for viral uncoating. In various drug-poliovirus complexes reported earlier, no significant conformational changes were found in the structures of the capsid proteins. In the structures reported here, the strain of virus is relatively insensitive to these antivirals. Correspondingly, significant conformational changes are necessary to accommodate the drug. These conformational changes affect both the immediate vicinity of the drug binding site, and more distant loops located near the fivefold axis. In addition, small but concerted shifts of the centers of mass of the major capsid proteins consistently have been detected whose magnitudes are correlated inversely with the effectiveness of the drugs. Collectively, the drug complexes appear to sample the conformational repertoire of poliovirus near equilibrium, and thus provide a possible model for the earliest stages of viral uncoating during infection.
About this Structure
1PO1 is a Protein complex structure of sequences from Human poliovirus 1. Full crystallographic information is available from OCA.
Reference
Ligand-induced conformational changes in poliovirus-antiviral drug complexes., Hiremath CN, Filman DJ, Grant RA, Hogle JM, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):558-70. PMID:15299887
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