Department of Chemistry, Maynooth University
Computational Biophysics at Maynooth University
News.
Our new work on the conformational propensity of the p53-Cter featured on the cover of issue 19(32) of PCCP. Click on the image to retrieve the paper
Computer simulations contribute to the discovery of a newly evolved functional interaction of the polycomb-like protein 1 (PCL1) with the tumor suppressor p53
Friday, October 30th, 2015
Polycomb-like proteins 1–3 (PCL1–3) are key epigenetic determinants for the maintenance of cellular identity, the regulation of differentiation, and have been linked to the occurrence of different forms of cancer. The evolutionary advantage of having three proteins with an apparent functional redundancy in mammals is unclear. A collaborative research effort lead by Dr Adrian Bracken at the Smurfit Institute of Genetics in TCD, and now published in Genes and Development (doi:10.1101/gad.267930.115) has put a significant step forward in illustrating the functional bifurcation of PCL proteins. In this work extensive biomolecular simulations, conducted by Dr Elisa Fadda in Maynooth Department of Chemistry, were instrumental to pin-point the structural basis for this divergence. Structural data from molecular modeling allowed the identification of two unique serine residues, acquired during recent vertebrate evolution, that confer to PCL1 its distinctive p53 binding specificity.