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Default NMR structure of the human Mediator MED25 ACID domain.

NMR structure of the human Mediator MED25 ACID domain.

Related Articles NMR structure of the human Mediator MED25 ACID domain.

J Struct Biol. 2010 Oct 22;

Authors: Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, de Launoit Y, Sizun C, Guittet E, Villeret V, Monté D

MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed ?-barrel with seven strands (B1-B7) and three ?-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the ?-barrel, defined by strands B4-B7-B6.

PMID: 20974256 [PubMed - as supplied by publisher]



Source: PubMed
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