Fig. 5: Stabilizing interactions in the DBD of the Alvinella pompejana p53 homolog. | Cell Death & Disease

Fig. 5: Stabilizing interactions in the DBD of the Alvinella pompejana p53 homolog.

From: Evolutionary history of the p53 family DNA-binding domain: insights from an Alvinella pompejana homolog

Fig. 5

A, B Hydrophobic core of the A. pompejana DBD. Superposition of the A. pompejana DBD (green) onto the structure of human p53 DBD (gray; PDB code 2XWR) [79] in (A) and the structure of human p63 DBD (PDB code 3QYN; yellow) [82] in (B) shows key differences in the hydrophobic core of the A. pompejana protein. Most notably, a phenylalanine and a neighboring smaller hydrophobic amino acid have swapped places when comparing the A. pompejana and the human DBDs (residues 255 and 270 in human p53). A non-saturated hydrogen bond found in the hydrophobic core of the human protein (orange dotted line) is replaced by equivalent hydrophobic residues seen in the human p63/p73 structure. C Superposition of the A. pompejana p53 DBD onto the structure of the superstable quadruple mutant M133L/V203A/N239Y/N268D of human p53 (PDB code 1UOL; gray) [55] shows a phenylalanine in the A. pompejana structure at the position of the stabilizing N239Y substitution in human p53 next to the zinc-binding site. D The same superposition as in panel C but focusing on the location of the cysteine cluster in the human protein shows that this cysteine cluster is absent in the A. pompejana DBD. Cys124 in the human p53 DBD is substituted by tryptophan in the A. pompejana DBD.

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