Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
A strategy for targeting protein kinases with large ATP-binding sites by using bulky and rigid octahedral ruthenium complexes as structural scaffolds is presented. A highly potent and selective GSK3 and Pim1 half-sandwich complex NP309 was successfully converted into a PAK1 inhibitor by making use of the large octahedral compounds Lambda-FL172 and Lambda-FL411 in which the cyclopentadienyl moiety of NP309 is replaced by a chloride and sterically demanding diimine ligands. A 1.65 A cocrystal structure of PAK1 with Lambda-FL172 reveals how the large coordination sphere of the ruthenium complex matches the size of the active site and serves as a yardstick to discriminate between otherwise closely related binding sites.
Targeting large kinase active site with rigid, bulky octahedral ruthenium complexes.,Maksimoska J, Feng L, Harms K, Yi C, Kissil J, Marmorstein R, Meggers E J Am Chem Soc. 2008 Nov 26;130(47):15764-5. PMID:18973295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maksimoska J, Feng L, Harms K, Yi C, Kissil J, Marmorstein R, Meggers E. Targeting large kinase active site with rigid, bulky octahedral ruthenium complexes. J Am Chem Soc. 2008 Nov 26;130(47):15764-5. PMID:18973295 doi:10.1021/ja805555a
