1Q1V

Structure of the Oncoprotein DEK: a putative DNA-binding Domain Related to the Winged Helix Motif

1Q1V の概要

• エントリーDOI: 10.2210/pdb1q1v/pdb
• 分子名称: DEK protein (1 entity in total)
• 機能のキーワード: winged-helix motif, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P35659
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8265.65

構造登録者

Devany, M.,Kotharu, N.P.,Matsuo, H. (登録日: 2003-07-22, 公開日: 2004-08-10, 最終更新日: 2024-05-29)

主引用文献

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

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: 15238633
DOI: 10.1110/ps.04797104

実験手法

SOLUTION NMR