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  • Similar interactions of natural products with biosynthetic enzymes and therapeutic targets could explain why nature produces such a large proportion of existing drugs

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    Author(s)
    Kellenberger, Esther
    Hofmann, Andreas
    Quinn, Ronald J
    Griffith University Author(s)
    Quinn, Ronald J.
    Year published
    2011
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    Abstract
    Natural products are made by nature through interaction with biosynthetic enzymes. Natural products also exert their effect as drugs by interaction with proteins. Does the recognition of the natural product by biosynthetic enzymes translate to recognition of the therapeutic target? Molecular modelling of flavonoid biosynthetic enzymes and kinases with a series of natural product kinase inhibitors led to the development of the concept of Protein Fold Topology (PFT). PFT describes cavity recognition points unrelated to protein fold similarity. The topology or spatial properties are preserved even though there is deformation ...
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    Natural products are made by nature through interaction with biosynthetic enzymes. Natural products also exert their effect as drugs by interaction with proteins. Does the recognition of the natural product by biosynthetic enzymes translate to recognition of the therapeutic target? Molecular modelling of flavonoid biosynthetic enzymes and kinases with a series of natural product kinase inhibitors led to the development of the concept of Protein Fold Topology (PFT). PFT describes cavity recognition points unrelated to protein fold similarity. The topology or spatial properties are preserved even though there is deformation of the protein elements that participate in the protein-ligand interactions. We observe helices or b-strands as equivalent in providing the invariant topology for protein-ligand interaction. In this Highlight, we explore the question: Will PFT aid drug discovery or is it the reason natural products have drug properties?
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    Journal Title
    Natural Product Reports
    Volume
    28
    Issue
    9
    DOI
    https://doi.org/10.1039/C1NP00026H
    Copyright Statement
    © 2011 Royal Society of Chemistry. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal website for access to the definitive, published version.
    Subject
    Chemical sciences
    Medicinal and biomolecular chemistry not elsewhere classified
    Biological sciences
    Structural biology (incl. macromolecular modelling)
    Biomedical and clinical sciences
    Publication URI
    http://hdl.handle.net/10072/42242
    Collection
    • Journal articles

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