Glycogen synthase kinase-3β (GSK-3β) structure. GSK-3β is a 433 residue protein consisting of 3 distinct structural domains. The N-terminal domain (yellow) consists of the first 134 residues and forms a 7-strand β-barrel. A short linker from the N-terminal domain, residues 135–151 connect the N-terminal domain to the α-helical domain (magenta). The α-helical domain is composed of residues 152–342. Sandwiched between the N-terminal and α-helical domain is the ATP-binding site. The C-terminal domain consists of residues 343–433 (blue). A strand diagram of GSK-3β. Phosphorylation of Ser-9 inactivates the enzyme, while phosphorylation of Tyr-216 activates. The p53 association region and basic domain region are both located in the N-terminal domain. Image was made using PyMol Molecular Graphics Software version 1.3 with the PDB structure 1UV5.
