2RVB

Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain

2RVB の概要

• エントリーDOI: 10.2210/pdb2rvb/pdb
• NMR情報: BMRB: 11594
• 分子名称: DNA repair protein complementing XP-C cells, General transcription factor IIH subunit 1 (2 entities in total)
• 機能のキーワード: dna repair, human xpc, acidic domain, general transcription factor, human tfiih p62, ph domain, dna binding protein-transcription complex, dna binding protein/transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q01831 P32780
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18375.61

構造登録者

Okuda, M.,Nishimura, Y. (登録日: 2015-07-01, 公開日: 2015-09-09, 最終更新日: 2024-05-01)

主引用文献

Okuda, M.,Kinoshita, M.,Kakumu, E.,Sugasawa, K.,Nishimura, Y.
Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC.
Structure, 23:1827-1837, 2015

PubMed Abstract: In global genome repair (GGR), XPC detects damaged nucleotides and recruits TFIIH complex. The small acidic region of XPC binds to the pleckstrin homology (PH) domain of TFIIH subunit p62; however, the recognition mechanism remains elusive. Here, we use nuclear magnetic resonance to present the tertiary structure of XPC bound to the PH domain. The XPC acidic region forms a long string stabilized by insertion of Trp133 and Val136 into two separate hollows of the PH domain, coupled with extensive electrostatic contacts. Analysis of several XPC mutants revealed that particularly Trp133 is essential for binding to the PH domain. In cell lines stably expressing mutant XPC, alanine substitution at Trp133 or Trp133/Val136 compromised UV resistance, recruitment of TFIIH to DNA damage, and removal of UV-induced photoproducts from genomic DNA. These findings show how TFIIH complex is recruited by XPC to damaged DNA, advancing our understanding of the early stage of GGR.

PubMed: 26278177
DOI: 10.1016/j.str.2015.07.009

実験手法

SOLUTION NMR