1Q1V
Structure of the Oncoprotein DEK: a putative DNA-binding Domain Related to the Winged Helix Motif
Summary for 1Q1V
| Entry DOI | 10.2210/pdb1q1v/pdb |
| Descriptor | DEK protein (1 entity in total) |
| Functional Keywords | winged-helix motif, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P35659 |
| Total number of polymer chains | 1 |
| Total formula weight | 8265.65 |
| Authors | Devany, M.,Kotharu, N.P.,Matsuo, H. (deposition date: 2003-07-22, release date: 2004-08-10, Last modification date: 2024-05-29) |
| Primary citation | Devany, M.,Kotharu, N.P.,Matsuo, H. Solution NMR structure of the C-terminal domain of the human protein DEK PROTEIN SCI., 13:2252-2259, 2004 Cited by PubMed Abstract: The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these clinical connections has yet to be explained. We have identified a structural domain in the C-terminal region of DEK [DEK(309-375)]. DEK(309-375) implies clinical importance because it can reverse the characteristic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. We determined the solution structure of DEK(309-375) by nuclear magnetic resonance spectroscopy, and found it to be structurally homologous to the E2F/DP transcription factor family. On the basis of this homology, we tested whether DEK(309-375) could bind DNA and identified the DNA-interacting surface. DEK presents a hydrophobic surface on the side opposite the DNA-interacting surface. The structure of the C-terminal region of DEK provides insights into the protein function of DEK. PubMed: 15238633DOI: 10.1110/ps.04797104 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
