2l23

NMR structure of the ACID (ACtivator Interacting Domain) of the human mediator Med25 protein

spinqualitylabelsall models 2l23 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l23 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease MED25_HUMAN Charcot-Marie-Tooth disease type 2B2. The disease is caused by mutations affecting the gene represented in this entry. Function MED25_HUMAN Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for RARA/RXRA-mediated transcription. Publication Abstract from PubMed 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 beta-barrel with seven strands (Beta1-Beta7) and three alpha-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 beta-barrel, defined by strands B4-B7-B6. NMR structure of the human Mediator MED25 ACID domain.,Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, Launoit YD, Sizun C, Guittet E, Villeret V, Monte D J Struct Biol. 2010 Oct 23. PMID:20974256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mediator

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