2ATA

Structural Basis of DNA Recognition by p53 Tetramers (complex II)

2ATA の概要

• エントリーDOI: 10.2210/pdb2ata/pdb
• 関連するPDBエントリー: 2AC0 2ADY 2AHI
• 分子名称: 5'-D(*AP*AP*GP*GP*CP*AP*TP*GP*CP*CP*TP*T)-3', Cellular tumor antigen p53, ZINC ION, ... (4 entities in total)
• 機能のキーワード: protein-dna complex, apoptosis-dna complex, apoptosis/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 104933.58

構造登録者

Kitayner, M.,Rozenberg, H.,Kessler, N.,Rabinovich, D.,Shakked, Z. (登録日: 2005-08-24, 公開日: 2006-07-11, 最終更新日: 2023-10-25)

主引用文献

Kitayner, M.,Rozenberg, H.,Kessler, N.,Rabinovich, D.,Shaulov, L.,Haran, T.E.,Shakked, Z.
Structural Basis of DNA Recognition by p53 Tetramers
Mol.Cell, 22:741-753, 2006

PubMed Abstract: The tumor-suppressor protein p53 is among the most effective of the cell's natural defenses against cancer. In response to cellular stress, p53 binds as a tetramer to diverse DNA targets containing two decameric half-sites, thereby activating the expression of genes involved in cell-cycle arrest or apoptosis. Here we present high-resolution crystal structures of sequence-specific complexes between the core domain of human p53 and different DNA half-sites. In all structures, four p53 molecules self-assemble on two DNA half-sites to form a tetramer that is a dimer of dimers, stabilized by protein-protein and base-stacking interactions. The protein-DNA interface varies as a function of the specific base sequence in correlation with the measured binding affinities of the complexes. The new data establish a structural framework for understanding the mechanisms of specificity, affinity, and cooperativity of DNA binding by p53 and suggest a model for its regulation by regions outside the sequence-specific DNA binding domain.

PubMed: 16793544
DOI: 10.1016/j.molcel.2006.05.015

実験手法

X-RAY DIFFRACTION (2.2 Å)