Figure 6

Atypical pTyr recognition proteins . On the left panels, molecular surface of each protein is overlaid on ribbon representation. (A) The C2 domain from the human PKCδ bound to a pTyr-peptide (PDB ID: 1YRK) [145]. The peptide is shown as grey sticks. Positively charged residues (green sticks) of the C2 domain that engage the pTyr moiety are shown to highlight the histidine-phenyl ring stacking feature. (B) pTyr binding by the human RKIP (PDB ID: 2QYQ) [149]. The structure features a deep pocket complementary to the pTyr side chain. The structure also highlights the lack of lysine and arginine in the binding pocket. (C) The homo-tetrameric active form of the human PKM2 bound to FBP (PDB ID: 3BJF) [150]. Each monomer is depicted with a different colour. The allosteric activator FBP is drawn as space-filling models. The distal active site from a monomer is identified with a blue circle. In the inset, the "lip" of the FBP-binding pocket created by the Lys433 and Trp482 residues and a loop region is coloured green. A pTyr ligand also binds to this region, and promotes the release of the FBP molecule, which results in inactivation of PKM2.