2RUK

Solution structure of the complex between p53 transactivation domain 2 and TFIIH p62 PH domain

2RUK の概要

• エントリーDOI: 10.2210/pdb2ruk/pdb
• NMR情報: BMRB: 11578
• 分子名称: Cellular tumor antigen p53, General transcription factor IIH subunit 1 (2 entities in total)
• 機能のキーワード: antitumor protein, general transcription factor, ph domain, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 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; Nucleus: P32780
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15175.05

構造登録者

Okuda, M.,Nishimura, Y. (登録日: 2014-09-24, 公開日: 2014-10-15, 最終更新日: 2024-10-16)

主引用文献

Okuda, M.,Nishimura, Y.
Extended string binding mode of the phosphorylated transactivation domain of tumor suppressor p53.
J.Am.Chem.Soc., 136:14143-14152, 2014

PubMed Abstract: The transactivation domain (TAD) of tumor suppressor p53 has homologous subdomains, TAD1 and TAD2. Both are intrinsically disordered in their free states, but all structures of TAD1 and TAD2 bound to their target proteins have demonstrated use of an amphipathic α-helix, suggesting that the binding-coupled helix folding mechanism of TAD1 and TAD2 is essential. Although phosphorylation of TAD is important to switch the function of p53, bound structures of phosphorylated TAD1 and TAD2 have not been determined. Here, we reveal the recognition mechanism of the phosphorylated TAD2 bound to a pleckstrin homology (PH) domain from human TFIIH subunit p62 in an extended string-like conformation. This string-like binding mode of TAD2 seems to be independent of its phosphorylation in spite of enhanced binding activity upon phosphorylation. This is in contrast to the amphipathic helical binding mode of the unphosphorylated TAD2 to the yeast tfb1 PH domain and demonstrates that the p53 TAD2 has much higher conformational malleability than previously appreciated.

PubMed: 25216154
DOI: 10.1021/ja506351f

実験手法

SOLUTION NMR