5OBR

Aurora A kinase in complex with 2-(3-chloro-5-fluorophenyl)quinoline-4-carboxylic acid and JNJ-7706621

Summary for 5OBR

• Entry DOI: 10.2210/pdb5obr/pdb
• Descriptor: Aurora kinase A, 2-(3-chloranyl-5-fluoranyl-phenyl)quinoline-4-carboxylic acid, 4-({5-amino-1-[(2,6-difluorophenyl)carbonyl]-1H-1,2,4-triazol-3-yl}amino)benzenesulfonamide, ... (5 entities in total)
• Functional Keywords: inhibitor, kinase, allostery, protein-protein interface, cell cycle
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : O14965
• Total number of polymer chains: 1
• Total formula weight: 32176.51

Authors

Rossmann, M.,Janecek, M.,Hyvonen, M. (deposition date: 2017-06-29, release date: 2017-08-09, Last modification date: 2024-05-08)

Primary citation

Cole, D.J.,Janecek, M.,Stokes, J.E.,Rossmann, M.,Faver, J.C.,McKenzie, G.J.,Venkitaraman, A.R.,Hyvonen, M.,Spring, D.R.,Huggins, D.J.,Jorgensen, W.L.
Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase-TPX2 protein-protein interaction.
Chem. Commun. (Camb.), 53:9372-9375, 2017

PubMed 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.

PubMed: 28787041
DOI: 10.1039/c7cc05379g

Experimental method

X-RAY DIFFRACTION (2.62 Å)