Fig. 4: Structural analysis shows p53 and pro-apoptotic Bax binding at the same pocket of BCL-2. | Nature Communications

Fig. 4: Structural analysis shows p53 and pro-apoptotic Bax binding at the same pocket of BCL-2.

From: Structures of p53/BCL-2 complex suggest a mechanism for p53 to antagonize BCL-2 activity

Fig. 4: Structural analysis shows p53 and pro-apoptotic Bax binding at the same pocket of BCL-2.

a Superposition of the BCL-2 structure in the p53-DBD/BCL-2 complex with the BCL-2 structure in the BCL-2/Bax-BH3 complex (PDB: 2XA0). BCL-2 and p53 in the p53-DBD/BCL-2 complex are colored hot pink and green, respectively. BCL-2 and Bax-BH3 in the BCL-2/Bax-BH3 complex are colored pink and light blue, respectively. b Superposition of BCL-2 structures shows the BH3-binding pockets. c, d The electrostatic surface potential of the BCL-2 molecule shows BCL-2/Bax-BH3 interactions (c) or BCL-2/p53-DBD interactions (d). The black box indicates the hydrophobic pockets of BCL-2. e, f The interfacial BCL-2 residues in the BCL-2/Bax-BH3 structure (e) or BCL-2/p53-DBD structure (f). Residues are colored and labelled as indicated.

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