Table of Contents
Journal of Cancer Research
Volume 2015, Article ID 762716, 15 pages
http://dx.doi.org/10.1155/2015/762716
Research Article

Molecular Docking Study Characterization of Rare Flavonoids at the Nac-Binding Site of the First Bromodomain of BRD4 (BRD4 BD1)

Department of Pharmacology, Amrita School of Pharmacy, Amrita Vishwa Vidyapeetham University, AIMS Health Sciences Campus, Kochi, Kerala 682041, India

Received 27 September 2014; Revised 13 February 2015; Accepted 13 February 2015

Academic Editor: Daizo Yoshida

Copyright © 2015 Karthik Dhananjayan. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

ε-N-Acetylation of lysine residues (Kac) is one of the most frequently occurring posttranslational modifications (PTMs) which control gene transcription and a vast array of diverse cellular functions. Bromodomains are epigenetic regulators involved in posttranslational modification. In silico docking studies were carried out to evaluate the binding potential of selected rare flavonoids on to Nac binding site of BD1 domain of BRD4 BET family proteins. Rare flavonoids like 3-O-acetylpinobanksin, naringenin triacetate, and kaempferol tetraacetate were found to occupy the WPF shelf and at the same time they exhibited a better binding affinity with multiple crystal structures of first bromodomain BRD4 (BRD4 BD1) when compared with the known inhibitors.