2XNF

The Mediator Med25 activator interaction domain: Structure and cooperative binding of VP16 subdomains

2XNF の概要

• エントリーDOI: 10.2210/pdb2xnf/pdb
• 分子名称: MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 25 (1 entity in total)
• 機能のキーワード: transcription, activated transcription, mediator
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: Q71SY5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18284.30

構造登録者

Vojnic, E.,Mourao, A.,Seizl, M.,Simon, B.,Wenzeck, L.,Lariviere, L.,Baumli, S.,Meisterernst, M.,Sattler, M.,Cramer, P. (登録日: 2010-08-02, 公開日: 2011-03-09, 最終更新日: 2024-05-15)

主引用文献

Vojnic, E.,Mourao, A.,Seizl, M.,Simon, B.,Wenzeck, L.,Lariviere, L.,Baumli, S.,Baumgart, K.,Meisterernst, M.,Sattler, M.,Cramer, P.
Structure and Vp16 Binding of the Mediator Med25 Activator Interaction Domain.
Nat.Struct.Mol.Biol., 18:404-, 2011

PubMed Abstract: Eukaryotic transcription is regulated by interactions between gene-specific activators and the coactivator complex Mediator. Here we report the NMR structure of the Mediator subunit Med25 (also called Arc92) activator interaction domain (ACID) and analyze the structural and functional interaction of ACID with the archetypical acidic transcription activator VP16. Unlike other known activator targets, ACID forms a seven-stranded β-barrel framed by three helices. The VP16 subdomains H1 and H2 bind to opposite faces of ACID and cooperate during promoter-dependent activated transcription in a in vitro system. The activator-binding ACID faces are functionally required and conserved among higher eukaryotes. Comparison with published activator structures reveals that the VP16 activation domain uses distinct interaction modes to adapt to unrelated target surfaces and folds that evolved for activator binding.

PubMed: 21378965
DOI: 10.1038/NSMB.1997

実験手法

SOLUTION NMR