Figure 1
From: Tuning PFKFB3 Bisphosphatase Activity Through Allosteric Interference
The relative positions of the two targeted sites in PFKFB3 and the structural comparison to PFKFB2. (A,B) The top-down (A) and sideway (B) representations of the N-terminal β-hairpin structure (orange) and the compound 6 (green) bound in the secondary binding site of PFKFB3. The two monomers are shown in different colors (grey and blue). (C) Surface representation of the secondary binding site with compound 6 docked within. The PFKFB3 surface is coloured according to residue lipophilicity (green: lipophilic; purple: hydrophilic). (D) Is the PFKFB2 structure with one monomer (white) overlaid with the PFKFB3 structure in B. The shifting of the monomer in blue due to the lack of stable β-hairpin can lead to the loss of the secondary binding site found in PFKFB3.
