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  • 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)
    Quinn, Ronald J.
    McArdle, Bernadette M.
    Campitelli, Marc R.
    Year published
    2006
    Metadata
    Show full item record
    Abstract
    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
    http://pubs.acs.org/journal/jnprdf
    DOI
    https://doi.org/10.1021/np050229y
    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
    Medical and Health Sciences
    Publication URI
    http://hdl.handle.net/10072/13869
    Collection
    • Journal articles

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