A Common Protein Fold Topology Shared by Flavonoid Biosynthetic Enzymes and Therapeutic Targets.
Author(s)
McArdle, BM
Campitelli, MR
Quinn, RJ
Griffith University Author(s)
Year published
2006
Metadata
Show full item recordAbstract
The relationship between a natural product's biosynthetic enzyme and its therapeutic target is unknown. The concept of protein fold topologies, as a determining factor in recognition, has been developed through molecular modeling techniques. We have shown that biosynthetic enzymes and the therapeutic targets of three classes of natural products that inhibit protein kinases share a common protein fold topology (PFT) and cavity recognition points despite having different fold type classifications. The clinical agent flavopiridol would have been identified by this new approach.The relationship between a natural product's biosynthetic enzyme and its therapeutic target is unknown. The concept of protein fold topologies, as a determining factor in recognition, has been developed through molecular modeling techniques. We have shown that biosynthetic enzymes and the therapeutic targets of three classes of natural products that inhibit protein kinases share a common protein fold topology (PFT) and cavity recognition points despite having different fold type classifications. The clinical agent flavopiridol would have been identified by this new approach.
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Journal Title
Journal of Natural Products
Volume
69
Issue
1
Publisher URI
Copyright Statement
Self-archiving of the author-manuscript version is not yet supported by this publisher. The contents of this journal can be freely accessed online via the ACS web page after publication. Use hypertext link above to access the ACS website.
Subject
Chemical sciences
Biological sciences
Biomedical and clinical sciences