2IWI

CRYSTAL STRUCTURE OF THE HUMAN PIM2 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU1

Summary for 2IWI

• Entry DOI: 10.2210/pdb2iwi/pdb
• Descriptor: SERINE/THREONINE-PROTEIN KINASE PIM-2, RUTHENIUM-PYRIDOCARBAZOLE-1 (2 entities in total)
• Functional Keywords: nucleotide-binding, serine/threonine-protein kinase, pim2, kinase, cancer, leukemia, transferase, atp-binding, proto-oncogene, phosphorylation
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 69593.63

Authors

Russo, S.,Debreczeni, J.E.,Amos, A.,Bullock, A.N.,Fedorov, O.,Niesen, F.,Sobott, F.,Turnbull, A.,Pike, A.C.W.,Ugochukwu, E.,Papagrigoriou, E.,Bunkoczi, G.,Gorrec, F.,Edwards, A.,Arrowsmith, C.,Weigelt, J.,Sundstrom, M.,von Delft, F.,Knapp, S. (deposition date: 2006-06-30, release date: 2006-08-02, Last modification date: 2023-12-13)

Primary citation

Bullock, A.N.,Russo, S.,Amos, A.,Pagano, N.,Bregman, H.,Debreczeni, J.E.,Lee, W.H.,von Delft, F.,Meggers, E.,Knapp, S.
Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor.
PLoS ONE, 4:e7112-e7112, 2009

PubMed 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.

PubMed: 19841674
DOI: 10.1371/journal.pone.0007112

Experimental method

X-RAY DIFFRACTION (2.8 Å)