期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 16, 期 1, 页码 45-50出版社
SPRINGER
DOI: 10.1007/s00775-010-0699-x
关键词
Ruthenium; Half-sandwich; Protein kinase; Inhibitor
The 3.15-angstrom-resolution crystal structure of the R enantiomer of the highly bioactive and antiproliferative half-sandwich ruthenium complex DW12 bound to the ATP binding site of glycogen synthase kinase 3 beta (GSK-3 beta) is reported and the binding is compared with the GSK-3 beta binding of staurosporine and other organic inhibitors. The structure reveals a close packing of the organometallic inhibitor in the ATP binding site of GSK-3 beta via an induced-fit mechanism. The molecular structure of (R)-DW12 with the CO ligand oriented perpendicular to the pyridocarbazole heterocycle allows the complex to stretch the whole distance sandwiched between the faces of the Nand C-terminal lobes and to interact tightly with the flexible glycine-rich loop, which is uncommon for the interaction of GSK-3 beta with organic inhibitors.
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