Structural aspects of the p53 protein in relation to gene evolution: a second look.
Several years ago, a comparison of the amino acid sequences of p53 proteins from a variety of species enabled us to reveal structural features of this protein, giving clues to its function. Since then, numerous studies on the biochemical, immunological and biological functions of p53 as well as on its structure (including crystallography data) have provided considerable insight into the multifunctional aspects of p53. The purpose of this review is to present the most recent data concerning the various structural features of the p53 protein with special emphasis on its flexibility, which plays a key role in regulation of its biological activity.
Soussi
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Unité 301 INSERM, Paris, France.
May
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017124:Conserved Sequence; D006224:Cricetinae; D019143:Evolution, Molecular; D016158:Genes, p53; D008969:Molecular Sequence Data; D010802:Phylogeny; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000378:metabolism
D016159:Tumor Suppressor Protein p53