Substrate binding to Src: A new perspective on tyrosine kinase substrate recognition from NMR and molecular dynamics.

ABSTRACT: Most signal transduction pathways in humans are regulated by protein kinases through phosphorylation of their protein substrates. Typical eukaryotic protein kinases are of two major types: those that phosphorylate-specific sequences containing tyrosine (~90 kinases) and those that phosphorylate either serine or threonine (~395 kinases). The highly conserved catalytic domain of protein kinases comprises a smaller N lobe and a larger C lobe separated by a cleft region lined by the activation loop. Prior studies find that protein tyrosine kinases recognize peptide substrates by binding the polypeptide chain along the C-lobe on one side of the activation loop, while serine/threonine kinases bind their substrates in the cleft and on the side of the activation loop opposite to that of the tyrosi

SUBMITTER: Joshi MK 

PROVIDER: S-EPMC6954736 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature