Fig. 3.

Schematic representation of the transactivity of p53 mutants within the tetramerization domain. (a) The transactivities of 204 p53 mutants within residues 323–356 were mapped on the primary structure. (b–d) Residues affected by at least one type of amino acid substitution were mapped on the 3D structure (National Center for Biotechnology Information 3SAK file visualized by swiss-pdb viewer; ref. 20) of the tetramerization domain. The backbone structure (ribbon) is green (affected residues) or red (unaffected residues). (b) Right side view. The side chains of ten affected residues in theα-helix are shown. (c) Top view. The side chains of five affected residues in the β-strand are shown. (d) Front view. The side chains of three affected arginine residues are shown.