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. 2018 Feb 9;9(17):13713–13732. doi: 10.18632/oncotarget.24459

Figure 7.

Figure 7

(A) Alanine Scanning: Results summary for BioLuminate alanine scanning of interface residues of NKX2.5-GATA4 protein complex and change in binding free energy/affinity (ΔΔGb) (kcal/mol). Residue participated in the polar interaction (PI), shown as red bar and rest all other interface residue (OTH), shown as green bar. ΔΔGbvalue higher than zero means decrease in binding affinity and value less than zero means increase in binding affinity. Upper panel belongs to NKX2.5, and lower panel belongs to GATA4. (B) 2D interaction map of D16: 2D map represent the changes in interaction pattern of D16/N16 and R260/Q260 in wild type and Mutant form at BR1 site. (1 and 2) Interaction-map, within 5 Å from NKX2.5 residue: 1) D16; 2) N16. (3 and 4) Interaction-map, within 5 Å from GATA4 residue: 3) R260; 4) Q260. (C) Schematic representation: Key residue interactions of D16N@NKX2.5:R260Q@GATA4 and their physiological outcomes.