2KKJ
Solution structure of the Nuclear coactivator binding domain of CBP
2KKJ の概要
エントリーDOI | 10.2210/pdb2kkj/pdb |
関連するPDBエントリー | 1JJS 1KBH 1zoq 2c52 |
NMR情報 | BMRB: 16363 |
分子名称 | CREB-binding protein (1 entity in total) |
機能のキーワード | creb binding protein, ibid, nuclear coactivator domain, cbp, p160, transcription |
由来する生物種 | Mus musculus (mouse) |
細胞内の位置 | Cytoplasm (By similarity): P45481 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 6568.56 |
構造登録者 | |
主引用文献 | Kjaergaard, M.,Teilum, K.,Poulsen, F.M. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP Proc.Natl.Acad.Sci.USA, 107:12535-12540, 2010 Cited by PubMed Abstract: 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. PubMed: 20616042DOI: 10.1073/pnas.1001693107 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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