1JJS
NMR Structure of IBiD, A Domain of CBP/p300
Summary for 1JJS
| Entry DOI | 10.2210/pdb1jjs/pdb |
| Descriptor | CREB-BINDING PROTEIN (1 entity in total) |
| Functional Keywords | transcription regulation, coactivator, transcription |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm (By similarity): P45481 |
| Total number of polymer chains | 1 |
| Total formula weight | 5584.50 |
| Authors | Lin, C.H.,Hare, B.J.,Wagner, G.,Harrison, S.C.,Maniatis, T.,Fraenkel, E. (deposition date: 2001-07-09, release date: 2001-10-03, Last modification date: 2024-05-22) |
| Primary citation | Lin, C.H.,Hare, B.J.,Wagner, G.,Harrison, S.C.,Maniatis, T.,Fraenkel, E. A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol.Cell, 8:581-590, 2001 Cited by PubMed Abstract: The transcriptional coactivators CBP and p300 are critical regulators of metazoan gene expression. They associate with many different DNA-bound transcription factors through small, conserved domains. We have identified a compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (IBiD), and we have determined its structure by NMR. It has a helical framework containing an apparently flexible polyglutamine loop that participates in ligand binding. Spectroscopic data indicate that induced folding accompanies association of IBiD with its partners, which exhibit no evident sequence similarities. We demonstrate the significance both in vitro and in vivo of interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300. PubMed: 11583620DOI: 10.1016/S1097-2765(01)00333-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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