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.
Publication types
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Evaluation Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Binding Sites
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Enzyme Activation
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Microfluidic Analytical Techniques / methods*
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Peptide Library*
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Phosphorylation
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Protein Binding
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Protein Interaction Mapping / methods*
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Protein Serine-Threonine Kinases / analysis
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Protein Serine-Threonine Kinases / chemistry*
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Protein Serine-Threonine Kinases / metabolism*
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Sequence Analysis, Protein / methods*
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Substrate Specificity
Substances
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Peptide Library
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Protein Serine-Threonine Kinases