p38 MAPK
p38 Mitogen
Activated Protein Kinase
ATP binding site (or chemical binding site)
This site is present on the catalytic subunit of the MAPK. It catalyzes the transfer of the gamma phosphate from the ATP molecule to the amino acid.
KIM (Kinase Interaction Motif) docking site or polypeptide binding site allows specific recognition of the substrate by the MAPK. The KIM usually consists of approximately 10-50 amino acids and usually lies upstream of the phosphorylation site
Activation loop
The activation loop (or A-loop) is also referred to as the regulatory T-loop. Phosphorylation of threonine, serine, or tyrosine residues within the A-loop is required for full activation of most protein kinases. Most MAPKs contain a TxY phosphorylation motif in the activation loop, which is targeted by MAP2Ks, leading to the activation of the kinase.
Active site
Includes ATP binding and substrate binding sites, allowing it to catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Based on the structure of human CDK2 bound with ATP and substrate peptide, and on structures of p38alpha bound with inhibitors.
Polypeptide substrate binding site
