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Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction.

Published version
Peer-reviewed

Repository URI

https://www.repository.cam.ac.uk/handle/1810/277062

Repository DOI

https://doi.org/10.17863/CAM.17664
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Published version (1.91 MB)

Type

Article

Change log

Authors

Cole, Daniel J  ORCID logo  https://orcid.org/0000-0003-2933-0719
Janecek, Matej  ORCID logo  https://orcid.org/0000-0003-0740-641X
Rossmann, Maxim  ORCID logo  https://orcid.org/0000-0001-8811-3277

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

Volume Title

53

Publisher

Royal Society of Chemistry (RSC)

Publisher DOI

https://doi.org/10.1039/c7cc05379g

Rights and licensing

Attribution 4.0 International
Except where otherwised noted, this item's license is described as Attribution 4.0 International
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)

Collections

Scholarly Works - Biochemistry