Abstract
High throughput screening drug discovery utilizes large and expensive compound libraries. As an alternative, a smaller targeted library can be constructed with the aid of the 3D structure of the target molecule. We used the X-ray crystal structure of a protein homologous to the selected target in creation of a small focused library and evaluated inhibition potential of this library against Chlamydia pneumoniae, a common pathogen recently linked to atherosclerosis and risk of myocardial infarction.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetamides / chemical synthesis
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Acetamides / chemistry
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Acetamides / pharmacology
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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology
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Bacillus subtilis / enzymology
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Benzamides / chemical synthesis
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Benzamides / chemistry
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Benzamides / pharmacology
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Benzimidazoles / chemical synthesis
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Benzimidazoles / chemistry
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Benzimidazoles / pharmacology
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Binding Sites
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Cell Line
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Cell Survival / drug effects
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Chlamydophila pneumoniae / drug effects*
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Chlamydophila pneumoniae / enzymology
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Crystallography, X-Ray
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Databases, Factual*
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Drug Design*
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Humans
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Ligands
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Methyltransferases / antagonists & inhibitors*
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Methyltransferases / chemistry*
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Models, Molecular
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Oxadiazoles / chemical synthesis
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Oxadiazoles / chemistry
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Oxadiazoles / pharmacology
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Protein Conformation
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Pyridines / chemical synthesis
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Pyridines / chemistry
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Pyridines / pharmacology
Substances
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Acetamides
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Anti-Bacterial Agents
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Benzamides
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Benzimidazoles
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Ligands
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Oxadiazoles
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Pyridines
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Methyltransferases
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16S rRNA (adenine(1518)-N(6)-adenine(1519)-N(6))-dimethyltransferase