 |
PDBsum entry 1q1v
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
1q1v
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Solution nmr structure of the c-Terminal domain of the human protein dek.
|
|
|
Authors
|
|
M.Devany,
N.P.Kotharu,
H.Matsuo.
|
|
|
Ref.
|
|
Protein Sci, 2004,
13,
2252-2259.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
