Figure 1

The computer modeling and docking of p53 peptide involved in interaction with FAK and small molecules targeting FAK-p53 interaction. A. The secondary structure of p53 peptide (43–73 aa) predicted with PHYRE (Protein Homology/analogy recognition engine), as described [34]. The 7 amino-acid p53 peptide (65–72 amino acids of p53) found to be involved in interaction with FAK [20] is shown by grey color. B. The docking of the 7 amino acid p53 peptide involved in interaction with FAK inside the crystal structure of FAK-NT (N-terminal domain of FAK). The amino acids of FAK-NT interacting with the 7 amino acid p53 peptide are shown in white color. C. Zoomed image of FAK-NT interaction with the 7 amino acid p53 peptide. The amino-acids of FAK interacting with p53 peptide: R86, V95, W97, R125, I126, R127, L129, F147, Q150, D154, E256, F258, K259, P332, I336 and N339. D. Small molecules targeting FAK-p53 interaction. Screening of NCI small molecule database with DOCK5.1 program identified small molecules (called R compounds) docked into the region of FAK and p53 interaction. The purple color marks small molecule spheres. Peptide is shown by blue color and FAK-NT by green color.