High-throughput profiling of sequence recognition by tyrosine kinases and SH2 domains using bacterial peptide display.

ABSTRACT: Tyrosine kinases and SH2 (phosphotyrosine recognition) domains have binding specificities that depend on the amino acid sequence surrounding the target (phospho)tyrosine residue. Although the preferred recognition motifs of many kinases and SH2 domains are known, we lack a quantitative description of sequence specificity that could guide predictions about signaling pathways or be used to design sequences for biomedical applications. Here, we present a platform that combines genetically encoded peptide libraries and deep sequencing to profile sequence recognition by tyrosine kinases and SH2 domains. We screened several tyrosine kinases against a million-peptide random library and used the resulting profiles to design high-activity sequences. We also screened several kinases against a librar

SUBMITTER: Li A 

PROVIDER: S-EPMC10065799 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature