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. Author manuscript; available in PMC: 2014 May 10.
Published in final edited form as: Curr Pharm Des. 2012;18(9):1173–1185. doi: 10.2174/138161212799436368

Figure 3.

Figure 3

A.) The inactive structure of ERK2 (PDB ID: 1ERK) shows the unphosphorylated T-X-Y motif (cyan) located on the activation loop (L12) of protein kinases (183T-E-Y185 for ERK1/2). B.) The active structure of ERK2 (PDB ID: 2ERK) has been phosphorylated on both the threonine and tyrosine residues that favor conformational rearrangements stabilized by electrostatic interactions between the negatively charged phosphorylated residues and positively charged arginine residues (grey).