2XNF

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

Summary for 2XNF

• Entry DOI: 10.2210/pdb2xnf/pdb
• Descriptor: MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 25 (1 entity in total)
• Functional Keywords: transcription, activated transcription, mediator
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus: Q71SY5
• Total number of polymer chains: 1
• Total formula weight: 18284.30

Authors

Vojnic, E.,Mourao, A.,Seizl, M.,Simon, B.,Wenzeck, L.,Lariviere, L.,Baumli, S.,Meisterernst, M.,Sattler, M.,Cramer, P. (deposition date: 2010-08-02, release date: 2011-03-09, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR