1PFJ

Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit

1PFJ の概要

• エントリーDOI: 10.2210/pdb1pfj/pdb
• 分子名称: TFIIH basal transcription factor complex p62 subunit (1 entity in total)
• 機能のキーワード: ph/ptb domain, structural proteomics in europe, spine, structural genomics, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P32780
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12306.32

構造登録者

Gervais, V.,Lamour, V.,Jawhari, A.,Frindel, F.,Wasielewski, E.,Thierry, J.C.,Kieffer, B.,Poterszman, A.,Structural Proteomics in Europe (SPINE) (登録日: 2003-05-27, 公開日: 2004-06-08, 最終更新日: 2024-05-22)

主引用文献

Gervais, V.,Lamour, V.,Jawhari, A.,Frindel, F.,Wasielewski, E.,Dubaele, S.,Egly, J.M.,Thierry, J.C.,Kieffer, B.,Poterszman, A.
TFIIH contains a PH domain involved in DNA nucleotide excision repair.
Nat.Struct.Mol.Biol., 11:616-622, 2004

PubMed Abstract: The human general transcription factor TFIIH is involved in both transcription and DNA repair. We have identified a structural domain in the core subunit of TFIIH, p62, which is absolutely required for DNA repair activity through the nucleotide excision repair pathway. Using coimmunoprecipitation experiments, we showed that this activity involves the interaction between the N-terminal domain of p62 and the 3' endonuclease XPG, a major component of the nucleotide excision repair machinery. Furthermore, we reconstituted a functional TFIIH particle with a mutant of p62 lacking the N-terminal domain, showing that this domain is not required for assembly of the TFIIH complex and basal transcription. We solved its three-dimensional structure and found an unpredicted pleckstrin homology and phosphotyrosine binding (PH/PTB) domain, uncovering a new class of activity for this fold.

PubMed: 15195146
DOI: 10.1038/nsmb782

実験手法

SOLUTION NMR