Summary
PDB 2WAJ deposited: 2009-02-08 modified: 2011-07-13
Title CRYSTAL STRUCTURE OF HUMAN JNK3 COMPLEXED WITH A 1-ARYL-3,4-DIHYDROISOQUINOLINE INHIBITOR
Authors Atkinson, F.L., Bax, B.D., Brown, M.J., Champigny, A.C., Christopher, J.A., Chuang, T.T., Jones, E.J., Mosley, J.E., Musgrave, J.R.
Method X-RAY DIFFRACTION
Structure factors resolution 2.4 rfactor 0.183 rfree 0.264
DPI 0.77 theoretical min: 0.33
Citations

A series of 1-aryl-3,4-dihydroisoquinoline inhibitors of JNK3 are described. Compounds 20 and 24 are the most potent inhibitors (pIC50 7.3 and 6.9, respectively in a radiometric filter binding assay), with 10- and 1000-fold selectivity over JNK2 and JNK1, respectively, and selectivity within the wider mitogen-activated protein kinase (MAPK) family against p38alpha and ERK2. X-ray crystallography of 16 reveals a highly unusual binding mode where an H-bond acceptor interaction with the hinge region is made by a chloro substituent.

Bioorg.Med.Chem.Lett. 2009 Apr; 19(8):2230- doi:10.1016/J.BMCL.2009.02.098

Cross References
Database source Identifier Description
ChEMBL Document CHEMBL1153754
PubMed 19303774 BMCLE8
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
2WAJ/0 2WAJ 0 monomer 0 1 1 2740