Output details
13 - Electrical and Electronic Engineering, Metallurgy and Materials
University of Central Lancashire
Kinetics, in silico docking, molecular dynamics, and MM-GBSA binding studies on prototype indirubins, KT5720, and staurosporine as phosphorylase kinase ATP-binding site inhibitors: The role of water molecules examined
This article was the cover story in issue 3 of volume 79, Proteins: Structure, Function & Bioinformatics. Kinase selectivity is an important consideration in the design of effective drug candidates targeting these enzymes. For phosphorylase kinase (PhK), the lack of experimental structural information has also been an obstacle to progress. KT5720 is a known selective inhibitor of PhK. The source of this selectivity was identified in this work. This finding, along with the new computational models of PhK bound with inhibitors, will aid and accelerate future drug design efforts targeting PhK.
