A Novel Mode of Gleevec Binding Is Revealed by the Structure of Spleen Tyrosine Kinase

• Published in: The Journal of biological chemistry Vol. 279; no. 53; pp. 55827 - 55832
• Main Authors: Atwell, Shane, Adams, Jason M., Badger, John, Buchanan, Michelle D., Feil, Ingeborg K., Froning, Karen J., Gao, Xia, Hendle, Jörg, Keegan, Kevin, Leon, Barbara C., Müller-Dieckmann, Hans J., Nienaber, Vicki L., Noland, Brian W., Post, Kai, Rajashankar, K.R., Ramos, Aurora, Russell, Marijane, Burley, Stephen K., Buchanan, Sean G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 31.12.2004; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Benzamides; Binding Sites; Catalysis; Catalytic Domain; Crystallography, X-Ray; Enzyme Precursors - chemistry; Hematopoietic Stem Cells - metabolism; Humans; Hydrogen Bonding; Imatinib Mesylate; Insecta; Intracellular Signaling Peptides and Proteins; Ligands; Models, Molecular; Mutation; Phosphorylation; Piperazines - pharmacology; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protein-Tyrosine Kinases - chemistry; Pyrimidines - pharmacology; Signal Transduction; Staurosporine - pharmacology; Syk Kinase; X-Rays

Spleen tyrosine kinase (Syk) is a non-receptor tyrosine kinase required for signaling from immunoreceptors in various hematopoietic cells. Phosphorylation of two tyrosine residues in the activation loop of the Syk kinase catalytic domain is necessary for signaling, a phenomenon typical of tyrosine k...