3EXJ

Crystal Structure of a p53 Core Tetramer Bound to DNA

3EXJ の概要

• エントリーDOI: 10.2210/pdb3exj/pdb
• 関連するPDBエントリー: 3EXL
• 分子名称: mouse p53 core domain, 5'-D(P*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DCP*DA)-3', 5'-D(*DTP*DTP*DGP*DAP*DGP*DCP*DAP*DTP*DGP*DCP*DTP*DC)-3', ... (6 entities in total)
• 機能のキーワード: protein-dna complex, acetylation, activator, anti-oncogene, apoptosis, cell cycle, covalent protein-rna linkage, cytoplasm, disease mutation, dna-binding, endoplasmic reticulum, metal-binding, methylation, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation, zinc, transcription-dna complex, transcription/dna
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm : P02340
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 52098.64

構造登録者

Malecka, K.A. (登録日: 2008-10-16, 公開日: 2008-12-16, 最終更新日: 2023-12-27)

主引用文献

Malecka, K.A.,Ho, W.C.,Marmorstein, R.
Crystal structure of a p53 core tetramer bound to DNA.
Oncogene, 28:325-333, 2009

PubMed Abstract: The tumor suppressor p53 regulates downstream genes in response to many cellular stresses and is frequently mutated in human cancers. Here, we report the use of a crosslinking strategy to trap a tetrameric p53 DNA-binding domain (p53DBD) bound to DNA and the X-ray crystal structure of the protein/DNA complex. The structure reveals that two p53DBD dimers bind to B form DNA with no relative twist and that a p53 tetramer can bind to DNA without introducing significant DNA bending. The numerous dimer-dimer interactions involve several strictly conserved residues, thus suggesting a molecular basis for p53DBD-DNA binding cooperativity. Surface residue conservation of the p53DBD tetramer bound to DNA highlights possible regions of other p53 domain or p53 cofactor interactions.

PubMed: 18978813
DOI: 10.1038/onc.2008.400

実験手法

X-RAY DIFFRACTION (2 Å)