Kinase peptide specificity: improved determination and relevance to protein phosphorylation.

ABSTRACT: Specificity of phosphorylation is critical to signal transduction. Recent emphasis on colocalization of substrate and kinase has eclipsed emphasis on peptide specificity, i.e., kinase preference for particular amino acids surrounding the phosphorylation site. We describe an approach to determining peptide specificity by using positional scanning of biotinylated oriented peptide libraries and insights emerging from those determinations. We accurately determine preference (or disfavor) for residues at a given substrate position (such as P+2) by comparison of in vitro phosphorylation of peptide libraries differing by a single residue at that position. By analysis of all positions near the phosphorylation site, position-specific scoring matrices are generated and used both to understand the ba

SUBMITTER: Fujii K 

PROVIDER: S-EPMC518827 | biostudies-literature | 2004 Sep

REPOSITORIES: biostudies-literature