Reversing allosteric communication: From detecting allosteric sites to inducing and tuning targeted allosteric response
Fig 8
Allosteric signalling from overlapping activator/inhibitor binding sites in PFK.
Perturbation of the larger binding site ADP (activator, red) causes larger increase in free energy (0.70 kcal/mol) to F6P functional sites, compared to that (0.30 kcal/mol) obtained from the smaller site PEP (inhibitor, blue). Residues in the sites are displayed as spheres along with the residue numbers. ADP and PEP from ligand-bound crystal structures (PDB code: 4pfk and 6pfk, respectively) are superimposed on the structure for illustration. The common residues that bind both ligands are colored grey, residues that only bind ADP are colored red. The distance cutoff for interacting residues of PFK and corresponding ligands is 3.5 Å.