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

ISSN: 1875-5992 (Online)
ISSN: 1871-5206 (Print)


Volume 16, 12 Issues, 2016


Download PDF Flyer




Anti-Cancer Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Cancer Agents

Aims & ScopeAbstracted/Indexed in

Ranking and Category:
  • 27th of 59 in Chemistry, Medicinal

Submit Abstracts Online Submit Manuscripts Online

Editor-in-Chief:
Michelle Prudhomme
Universite Blaise Pascal - C.N.R.S
Aubiere Cedex
France


View Full Editorial Board

Subscribe Purchase Articles Order Reprints

Current: 2.722
5 - Year: 2.849

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



Anti-Cancer Agents in Medicinal Chemistry, 8(6): 638-645.

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

Affiliation: Departamento de Farmacologia,Universidad de Alcala, Alcala de Henares, 28871 Madrid, Spain.

Abstract

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.



Download Free Order Reprints Order Eprints Rights and Permissions




Article Details

Volume: 8
Issue Number: 6
First Page: 638
Last Page: 645
Page Count: 8
DOI: 10.2174/187152008785133056
Advertisement

Related Journals




Webmaster Contact: urooj@benthamscience.org Copyright © 2016 Bentham Science