Fig. 6: Reshaping of the hydrophobic core of p53 family proteins during evolution. | Cell Death & Disease

Fig. 6: Reshaping of the hydrophobic core of p53 family proteins during evolution.

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

Fig. 6

A sequence alignment of vertebrate and invertebrate p53 family DBDs shows a switch of the packing pattern of the DBD hydrophobic core via residues 255 and 270. The aromatic swap illustrated in Fig. 5A appears to have occurred at the transition from invertebrates to vertebrates. Also highlighted is an unsaturated hydrogen-bond pair in the hydrophobic core of vertebrate p53 DBDs (residues 236 and 253, human p53 numbering). UniProt accession numbers are given after the name of each species. The numbering of the A. pompejana p53 homolog is based on the translation of EST N72937.

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