4CZ7

Truncated tetramerization domain of zebrafish p53 (crystal form III)

4CZ7 の概要

• エントリーDOI: 10.2210/pdb4cz7/pdb
• 関連するPDBエントリー: 4CZ5 4CZ6
• 分子名称: CELLULAR TUMOR ANTIGEN P53, PHOSPHATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cell cycle, tumor suppressor, transcription factor protein evolution, danio rerio
• 由来する生物種: DANIO RERIO (ZEBRAFISH)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 23172.63

構造登録者

Joerger, A.C. (登録日: 2014-04-16, 公開日: 2014-08-27, 最終更新日: 2024-05-08)

主引用文献

Joerger, A.C.,Wilcken, R.,Andreeva, A.
Tracing the Evolution of the P53 Tetramerization Domain
Structure, 22:1301-, 2014

PubMed Abstract: The tetrameric transcription factors p53, p63, and p73 evolved from a common ancestor and play key roles in tumor suppression and development. Surprisingly, p63 and p73 require a second helix in their tetramerization domain for the formation of stable tetramers that is absent in human p53, raising questions about the evolutionary processes leading to diversification. Here we determined the crystal structure of the zebrafish p53 tetramerization domain, which contains a second helix, reminiscent of p63 and p73, combined with p53-like features. Through comprehensive phylogenetic analyses, we systematically traced the evolution of vertebrate p53 family oligomerization domains back to the beginning of multicellular life. We provide evidence that their last common ancestor also had an extended p63/p73-like domain and pinpoint evolutionary events that shaped this domain during vertebrate radiation. Domain compaction and transformation of a structured into a flexible, intrinsically disordered region may have contributed to the expansion of the human p53 interactome.

PubMed: 25185827
DOI: 10.1016/J.STR.2014.07.010

実験手法

X-RAY DIFFRACTION (1.1 Å)