Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases
Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Comment:includes ATP binding and substrate binding sites
Structure:2WO6; Human DYRK1A binds D15 inhibitor and consensus substrate peptide; contacts at 4A.
Comment:also based on the structure of human CDK2 bound with ATP and substrate peptide, and on the structures of other CMGC kinases bound with ATP or ATP analogs
Jiyao W et al.(2023). "The conserved domain database in 2023.",