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Giant leap for p53, small step for drug design
Author(s) -
Anderson Mary E.,
Tegtmeyer Peter
Publication year - 1995
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950170103
Subject(s) - transactivation , dna , biology , suppressor , p53 protein , dna damage , microbiology and biotechnology , genetics , computational biology , gene , transcription factor
We review the findings of Cho et al. (1) on the crystal structure of a p53 tumor suppressor‐DNA complex. The core DNA binding domain of p53 folds into a structure termed a β‐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.