2kkj

Solution structure of the Nuclear coactivator binding domain of CBP

spinqualitylabelsall models 2kkj, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kkj is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1kbh, 1jjs, 2c52, 1zoq Activity: Histone acetyltransferase, with EC number 2.3.1.48 Resources: FirstGlance, OCA, RCSB, PDBsum Function [CBP_MOUSE] Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds into two remarkably different states depending on the ligand being ACTR or IRF-3. The ligand-free state of NCBD was characterized in order to understand the mechanism of folding upon ligand binding. Biophysical studies show that despite the molten globule nature of the domain, it contains a small cooperatively folded core. By NMR spectroscopy, we have demonstrated that the folded core of NCBD has a well ordered conformer with specific side chain packing. This conformer resembles the structure of the NCBD in complex with the protein ligand, ACTR, suggesting that ACTR binds to prefolded NCBD molecules from the ensemble of interconverting structures. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.,Kjaergaard M, Teilum K, Poulsen FM Proc Natl Acad Sci U S A. 2010 Jul 13;107(28):12535-40. Epub 2010 Jun 24. PMID:20616042 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CREB-binding protein

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