1S7E
Solution structure of HNF-6
Summary for 1S7E
| Entry DOI | 10.2210/pdb1s7e/pdb |
| Related | 1e3o |
| NMR Information | BMRB: 5678 |
| Descriptor | Hepatocyte nuclear factor 6 (1 entity in total) |
| Functional Keywords | transcription regulation, homeobox, dna-binding, nuclear protein, transcription |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: O08755 |
| Total number of polymer chains | 1 |
| Total formula weight | 17387.20 |
| Authors | |
| Primary citation | Sheng, W.,Yan, H.,Rausa, F.M.,Costa, R.H.,Liao, X. Structure of the hepatocyte nuclear factor 6alpha and its interaction with DNA. J.Biol.Chem., 279:33928-33936, 2004 Cited by PubMed Abstract: Hepatocyte nuclear factor 6 (HNF-6) belongs to the family of One Cut transcription factors (also known as OC-1) and is essential for the development of the mouse pancreas, gall bladder, and the interhepatic bile ducts. HNF-6 binds to DNA as a monomer utilizing a single cut domain and a divergent homeodomain motif located at its C terminus. Here, we have used NMR methods to determine the solution structures of the 162 amino acid residue DNA-binding domain of the HNF-6alpha protein. The resulting overall structure of HNF-6alpha has two different distinct domains: the Cut domain and the Homeodomain connected by a long flexible linker. Our NMR structure shows that the Cut domain folds into a topology homologous to the POU DNA-binding domain, even though the sequences of these two protein families do not show homology. The DNA contact sequence of the HNF-6alpha was mapped with chemical shift perturbation methods. Our data also show that a proposed CREB-binding protein histone acetyltransferase protein-recruiting sequence, LSDLL, forms a helix and is involved in the hydrophobic core of the Cut domain. The structure implies that this sequence has to undergo structural changes when it interacts with CREB-binding protein. PubMed: 15169783DOI: 10.1074/jbc.M403805200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
