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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3
Author(s) -
AtillaGokcumen G. Ekin,
Pagano Nicholas,
Streu Craig,
Maksimoska Jasna,
Filippakopoulos Panagis,
Knapp Stefan,
Meggers Eric
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800489
Subject(s) - gsk 3 , staurosporine , glycogen synthase , ruthenium , chemistry , biochemistry , binding site , kinase , gsk3b , enzyme , protein kinase a , biology , catalysis
Perfect match : An organoruthenium complex with at most a low picomolar binding constant for glycogen synthase kinases 3 is reported, whose binding to the ATP‐binding site has been analyzed by X‐ray crystallography. The complex, ( R Ru )‐ NP549 , is one of the most potent protein kinase inhibitors reported to date, almost four orders of magnitude more potent than the related natural product staurosporine.

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