title: Giant leap for p53, small step for drug design.
abstract: We review the findings of Cho et al. on the crystal structure of a p53 tumor suppressor-DNA complex. The core DNA binding domain of p53 folds into a structure termed a beta-sandwich, which organizes two loops and a loop-sheet-helix structure on one surface of p53 to interact with the consensus DNA recognition sequence of p53. These structures help to explain the functions of wild-type p53 and the effects of tumor-associated mutations on p53 DNA binding, transactivation and suppression of cellular proliferation.
authors.affiliation: Department of Molecular Genetics and Microbiology, State University of New York, Stony Brook 11794.
authors.forename: M E
authors.initials: ME
authors.lastname: Anderson
authors.forename: P
authors.initials: P
authors.lastname: Tegtmeyer
mesh_terms: D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000737:chemistry; D015195:Drug Design; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D017510:Protein Folding; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry*
chemical_list: D016159:Tumor Suppressor Protein p53; D004247:DNA