5odd
From Proteopedia
HUMAN MED26 N-TERMINAL DOMAIN (1-92)
Structural highlights
FunctionMED26_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 pre-initiation complex with RNA polymerase II and the general transcription factors. Publication Abstract from PubMedMED26 is a subunit of the Mediator, a very large complex involved in regulation of gene transcription by RNA Polymerase II. MED26 regulates the switch between initiation and elongation phases of the transcription. This function requires interaction of its N-terminal domain (NTD) with several protein partners implicated in transcriptional regulation. Molecular details of the structure and interaction mode of MED26 NTD would improve understanding of this complex regulation. As a first step towards structural characterization, sequence specific (1)H, (13)C and (15)N assignments for MED26 NTD was performed based on Nuclear Magnetic Resonance spectroscopy. TALOS+ analysis of the chemical shifts data revealed a domain solely composed of helices. Assignments will be further used to solve NMR structure and dynamics of MED26 NTD and investigate the molecular details of its interaction with protein partners. 1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26.,Peruzzini R, Lens Z, Verger A, Dewitte F, Ferreira E, Baert JL, Villeret V, Landrieu I, Cantrelle FX Biomol NMR Assign. 2016 Apr;10(1):233-6. doi: 10.1007/s12104-016-9673-z. Epub, 2016 Feb 9. PMID:26861138[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Cantrelle F-X | Dewitte F | Hanoulle X | Landrieu I | Lens Z | Perruzini R | Verger A | Villeret V
