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A rapid method for determining protein kinase phosphorylation specificity.

Jessica E Hutti·Emily T Jarrell·James D Chang·Derek W Abbott·Peter Storz·Alex Toker·Lewis C Cantley·Benjamin E Turk
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Abstract

Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

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Amino Acid MotifsBinding SitesEnzyme ActivationMicrofluidic Analytical TechniquesPeptide LibraryPhosphorylationProtein BindingProtein Interaction MappingProtein Serine-Threonine KinasesSequence Analysis, ProteinSubstrate SpecificityEvaluation StudyJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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Jessica E Hutti, Emily T Jarrell, James D Chang, Derek W Abbott, Peter Storz, Alex Toker, Lewis C Cantley, Benjamin E Turk. 2004. A rapid method for determining protein kinase phosphorylation specificity.. https://doi.org/10.1038/nmeth708

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