2l5e

Complex between BD1 of Brd3 and GATA-1 C-tailComplex between BD1 of Brd3 and GATA-1 C-tail

Structural highlights 2l5e is a 2 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BRD3_MOUSE Chromatin reader that recognizes and binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors (PubMed:21536911). Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (PubMed:21536911). Publication Abstract from PubMed Recent data demonstrate that small synthetic compounds specifically targeting bromodomain proteins can modulate the expression of cancer-related or inflammatory genes. Although these studies have focused on the ability of bromodomains to recognize acetylated histones, it is increasingly becoming clear that histone-like modifications exist on other important proteins, such as transcription factors. However, our understanding of the molecular mechanisms through which these modifications modulate protein function is far from complete. The transcription factor GATA1 can be acetylated at lysine residues adjacent to the zinc finger domains, and this acetylation is essential for the normal chromatin occupancy of GATA1. We have recently identified the bromodomain-containing protein Brd3 as a cofactor that interacts with acetylated GATA1 and shown that this interaction is essential for the targeting of GATA1 to chromatin. Here we describe the structural basis for this interaction. Our data reveal for the first time the molecular details of an interaction between a transcription factor bearing multiple acetylation modifications and its cognate recognition module. We also show that this interaction can be inhibited by an acetyllysine mimic, highlighting the importance of further increasing the specificity of compounds that target bromodomain and extraterminal (BET) bromodomains in order to fully realize their therapeutic potential. Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3.,Gamsjaeger R, Webb SR, Lamonica JM, Billin A, Blobel GA, Mackay JP Mol Cell Biol. 2011 Jul;31(13):2632-40. doi: 10.1128/MCB.05413-11. Epub 2011 May , 9. PMID:21555453 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bromodomain-containing protein 3D structures

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