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PROTEIN STRUCTURE REPORT

Solution NMR structure of the C-terminal domain of the human protein DEK

Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA

(RECEIVED April 7, 2004; FINAL REVISION May 3, 2004; ACCEPTED May 3, 2004)

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.

Keywords: NMR structure; oncogene product; ataxia-telangiectasia; acute myeloid leukemia; chromatin-associated protein; chromosomal translocation

Abbreviations: DEK(309–375), deletion of the N-terminal 308 amino acids of the human DEK protein • AML, acute myelogenous leukemia • A-T, ataxia telangiectasia • JRA, juvenile rheumatoid arthritis • HSQC, hetero-nuclear single quantum coherence • NOE, nuclear Overhauser effect • RMSD, root mean square deviation

Reprint requests to: Hiroshi Matsuo, Department of Biochemistry, Molecular Biology and Biophysics, 321 Church Street, S.E. Jackson Hall 6-155, University of Minnesota, Minneapolis, MN 55455, USA; e-mail: matsu029{at}umn.edu; fax: (612) 625-2163.

Supplemental material: see www.proteinscience.org

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04797104.

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				M. Devany, F. Kappes, K.-M. Chen, D. M. Markovitz, and H. Matsuo Solution NMR structure of the N-terminal domain of the human DEK protein Protein Sci., February 1, 2008; 17(2): 205 - 215. [Abstract] [Full Text] [PDF]