The Protein Kinase Inhibitor Balanol: Structure – Activity Relationships and Structure-Based Computational Studies

Author(s): Vineet Pande, Maria J. Ramos, Federico Gago

Journal Name: Anti-Cancer Agents in Medicinal Chemistry
(Formerly Current Medicinal Chemistry - Anti-Cancer Agents)

Volume 8 , Issue 6 , 2008

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Balanol, a fungal metabolite, is a potent ATP-competitive inhibitor of Protein Kinase C (PKC) and Protein Kinase A (PKA), important targets in oncology. Since its discovery in 1993, a number of studies have been performed in order to design selective and bioavailable balanol analogs. Several crystal structures of PKA in complex with balanol and a few analogs bound within the catalytic site have also been solved providing insight about the key interactions for binding. The PKA-balanol complex has also served as an interesting model system for structurebased ligand design and validation of a number of computational methodologies aimed at both understanding the physical basis for molecular recognition and addressing the important issue of protein flexibility in ligand binding. We provide an overview of the structure-activity relationships of balanol analogs and summarize the progress made in structural and computational studies involving balanol.

Keywords: Balanol, structure activity relationships, kinases, computational chemistry, x-ray crystal structure, protein flexibility, adenosine triphosphate

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Article Details

Year: 2008
Page: [638 - 645]
Pages: 8
DOI: 10.2174/187152008785133056

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