Ruthenium half-sandwich complexes bound to protein kinase Pim-1.
|Author||Debreczeni, Judit E; Bullock, Alex N; Atilla, G Ekin; et al|
|Subject||Crystallography, X-Ray Models, Molecular Protein Kinase Inhibitors Protein Structure, Tertiary Proto-Oncogene Proteins c-pim-1 Ruthenium Stereoisomerism chemistry chemistry metabolism chemistry metabolism|
Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor.
|Abstract||The serine/threonine kinase PIM2 is highly expressed in human leukemia and lymphomas and has been shown to positively regulate survival and proliferation of tumor cells. Its diverse ATP site makes PIM2 a promising target for the development of anticancer agents. To date our knowledge of catalytic domain structures of the PIM kinase family is limited to PIM1 which has been extensively studied and which shares about 50% sequence identity with PIM2.|
|Author||Bullock, Alex N; Russo, Santina; Amos, Ann; et al|
|Subject||Binding Sites Chemistry, Pharmaceutical Crystallography, X-Ray Drug Design Enzyme Inhibitors Humans Molecular Structure Protein Conformation Protein Isoforms Protein Structure, Tertiary Proto-Oncogene Proteins c-pim-1 Ruthenium Staurosporine Structure-Activity Relationship methods methods chemistry chemistry chemistry chemistry|