Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Stokes, Jamie E
Faver, John C
Abstract
Free energy perturbation theory, in combination with enhanced sampling of protein-ligand binding modes, is evaluated in the context of fragment-based drug design, and used to design two new small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction.
Description
Keywords
Aurora Kinase A, Cell Cycle Proteins, Humans, Microtubule-Associated Proteins, Models, Molecular, Molecular Dynamics Simulation, Molecular Structure, Nuclear Proteins, Protein Binding, Protein Kinase Inhibitors, Small Molecule Libraries
Journal Title
Chem Commun (Camb)
Conference Name
Journal ISSN
1359-7345
1364-548X
1364-548X
Volume Title
53
Publisher
Royal Society of Chemistry (RSC)
Publisher DOI
Sponsorship
MRC (unknown)
Wellcome Trust (090340/Z/09/Z)
Medical Research Council (G1001522)
Medical Research Council (MC_UU_12022/1)
Engineering and Physical Sciences Research Council (EP/K039520/1)
Medical Research Council (MR/L007266/1)
MRC (MC_UU_12022/8)
Wellcome Trust (090340/Z/09/Z)
Medical Research Council (G1001522)
Medical Research Council (MC_UU_12022/1)
Engineering and Physical Sciences Research Council (EP/K039520/1)
Medical Research Council (MR/L007266/1)
MRC (MC_UU_12022/8)