2rmu: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmu OCA], [http://www.ebi.ac.uk/pdbsum/2rmu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rmu RCSB]</span> | |||
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==About this Structure== | ==About this Structure== | ||
2RMU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ | 2RMU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_14 Human rhinovirus 14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMU OCA]. | ||
==Reference== | ==Reference== | ||
Three-dimensional structures of drug-resistant mutants of human rhinovirus 14., Badger J, Krishnaswamy S, Kremer MJ, Oliveira MA, Rossmann MG, Heinz BA, Rueckert RR, Dutko FJ, McKinlay MA, J Mol Biol. 1989 May 5;207(1):163-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2544734 2544734] | Three-dimensional structures of drug-resistant mutants of human rhinovirus 14., Badger J, Krishnaswamy S, Kremer MJ, Oliveira MA, Rossmann MG, Heinz BA, Rueckert RR, Dutko FJ, McKinlay MA, J Mol Biol. 1989 May 5;207(1):163-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2544734 2544734] | ||
[[Category: Human rhinovirus | [[Category: Human rhinovirus 14]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Badger, J.]] | [[Category: Badger, J.]] | ||
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[[Category: rhinovirus coat protein]] | [[Category: rhinovirus coat protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:11 2008'' | ||
Revision as of 05:02, 31 March 2008
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| , resolution 3.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURES OF DRUG-RESISTANT MUTANTS OF HUMAN RHINOVIRUS 14
OverviewOverview
Mutants of human rhinovirus 14 were isolated and characterized by searching for resistance to compounds that inhibit viral uncoating. The portions of the RNA that code for amino acids that surround the antiviral compound binding site were sequenced. X-ray analysis of two of these mutants, 1188 Val----Leu and 1199 Cys----Tyr, shows that these were single-site substitutions which would sterically hinder drug binding. Differences in the resistance of mutant viruses to various antiviral compounds may be rationalized in terms of the three-dimensional structures of these mutants. Predictions of the structures of mutant rhinovirus 14 with the substitutions 1188 Val----Leu, 1199 Cys----Tyr and 1199 Cys----Trp in VP1 were made using a molecular dynamics technique. The predicted structure of the 1199 Cys----Tyr mutant was consistent with the electron density map, while the 1188 Val----Leu prediction was not. Large (up to 1.4 A) conformational differences between native rhinovirus 14 and the 1199 Cys----Tyr mutant occurred in main-chain atoms near the mutation site. These changes, as well as the orientation of the 1199 tyrosine side-chain, were correctly predicted by the molecular dynamics calculation. The structure of the predicted 1199 Cys----Trp mutation is consistent with the drug-resistant properties of this virus.
About this StructureAbout this Structure
2RMU is a Protein complex structure of sequences from Human rhinovirus 14. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structures of drug-resistant mutants of human rhinovirus 14., Badger J, Krishnaswamy S, Kremer MJ, Oliveira MA, Rossmann MG, Heinz BA, Rueckert RR, Dutko FJ, McKinlay MA, J Mol Biol. 1989 May 5;207(1):163-74. PMID:2544734
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