PDBsum entry 1q1v

DNA binding protein

PDB id: 1q1v

Contents

Protein chain

70 a.a. *

* Residue conservation analysis

PDB id:

1q1v

Name:

DNA binding protein

Title:

Structure of the oncoprotein dek: a putative DNA-binding domain related to the winged helix motif

Structure:

Dek protein. Chain: a. Fragment: residues 309-378. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dek. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

M.Devany,N.P.Kotharu,H.Matsuo

Key ref:

M.Devany et al. (2004). Solution NMR structure of the C-terminal domain of the human protein DEK. Protein Sci, 13, 2252-2259. PubMed id: 15238633 DOI: 10.1110/ps.04797104

Date:

22-Jul-03 Release date: 10-Aug-04

Protein chain

P35659  (DEK_HUMAN) -  Protein DEK from Homo sapiens

Seq: 375 a.a.

Struc: 70 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.04797104

Protein Sci 13:2252-2259 (2004)

PubMed id: 15238633

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

M.Devany, N.P.Kotharu, H.Matsuo.

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.

Selected figure(s)

Figure 2.
Figure 2. (A) The stereoview of the three-dimensional structure of DEK(309-375) reveals a hydrophobic core. The backbone atoms of the 10 lowest energy structures are superimposed in this figure. This figure was prepared using MOLMOL (Koradi et al. 1996). (B) The structure of DEK(309-375) closely resembles that of DP2. The -helices of DEK(309-375; black) is superimposed onto the -helices of the DNA-binding domain of DP2 (gray). DEK(309-375) lacks the sheet present in DP2. This figure was prepared using MOLMOL (Koradi et al. 1996).

The above figure is reprinted by permission from the Protein Society: Protein Sci (2004, 13, 2252-2259) copyright 2004.

Figure was selected by the author.