2oi4
Crystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazoleCrystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazole
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA general route to ruthenium pyridocarbazole half-sandwich complexes is presented and applied to the synthesis of sixteen new compounds, many of which have modulated protein kinase inhibition properties. For example, the incorporation of a fluorine into the pyridine moiety increases the binding affinity for glycogen synthase kinase 3 by almost one order of magnitude. These data are supplemented with cyclic voltammetry experiments and a protein co-crystallographic study. Ruthenium half-sandwich complexes as protein kinase inhibitors: derivatization of the pyridocarbazole pharmacophore ligand.,Pagano N, Maksimoska J, Bregman H, Williams DS, Webster RD, Xue F, Meggers E Org Biomol Chem. 2007 Apr 21;5(8):1218-27. Epub 2007 Mar 20. PMID:17406720[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||