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

Publication ,  Journal Article
Devany, M; Kappes, F; Chen, K-M; Markovitz, DM; Matsuo, H
Published in: Protein science : a publication of the Protein Society
February 2008

The human DEK protein has a long-standing association with carcinogenesis since the DEK gene was originally identified in the t(6:9) chromosomal translocation in a subtype of patients with acute myelogenous leukemia (AML). Recent studies have partly unveiled DEK's cellular functions including apoptosis inhibition in primary cells as well as cancer cells, determination of 3' splice site of transcribed RNA, and suppression of transcription initiation by polymerase II. It has been previously shown that the N-terminal region of DEK, spanning residues 68-226, confers important in vitro and in vivo functions of DEK, which include double-stranded DNA (ds-DNA) binding, introduction of constrained positive supercoils into closed dsDNA, and apoptosis inhibition. In this paper, we describe the three-dimensional structure of the N-terminal domain of DEK (DEKntd) as determined using solution NMR. The C-terminal part of DEKntd, which contains a putative DNA-binding motif (SAF/SAP motif), folds into a helix-loop-helix structure. Interestingly, the N-terminal part of DEKntd shows a very similar structure to the C-terminal part, although the N-terminal and the C-terminal part differ distinctively in their amino acid sequences. As a consequence, the structure of DEKntd has a pseudo twofold plane symmetry. In addition, we tested dsDNA binding of DEKntd by monitoring changes of NMR chemical shifts upon addition of dsDNAs. We found that not only the C-terminal part containing the SAF/SAP motif but the N-terminal part is also involved in DEKntd's dsDNA binding. Our study illustrates a new structural variant and reveals novel dsDNA-binding properties for proteins containing the SAP/SAF motif.

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Published In

Protein science : a publication of the Protein Society

DOI

EISSN

1469-896X

ISSN

0961-8368

Publication Date

February 2008

Volume

17

Issue

2

Start / End Page

205 / 215

Related Subject Headings

  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Poly-ADP-Ribose Binding Proteins
  • Oncogene Proteins
  • Nuclear Magnetic Resonance, Biomolecular
  • Molecular Sequence Data
  • Humans
  • DNA-Binding Proteins
 

Citation

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Devany, M., Kappes, F., Chen, K.-M., Markovitz, D. M., & Matsuo, H. (2008). Solution NMR structure of the N-terminal domain of the human DEK protein. Protein Science : A Publication of the Protein Society, 17(2), 205–215. https://doi.org/10.1110/ps.073244108
Devany, Matthew, Ferdinand Kappes, Kuan-Ming Chen, David M. Markovitz, and Hiroshi Matsuo. “Solution NMR structure of the N-terminal domain of the human DEK protein.Protein Science : A Publication of the Protein Society 17, no. 2 (February 2008): 205–15. https://doi.org/10.1110/ps.073244108.
Devany M, Kappes F, Chen K-M, Markovitz DM, Matsuo H. Solution NMR structure of the N-terminal domain of the human DEK protein. Protein science : a publication of the Protein Society. 2008 Feb;17(2):205–15.
Devany, Matthew, et al. “Solution NMR structure of the N-terminal domain of the human DEK protein.Protein Science : A Publication of the Protein Society, vol. 17, no. 2, Feb. 2008, pp. 205–15. Epmc, doi:10.1110/ps.073244108.
Devany M, Kappes F, Chen K-M, Markovitz DM, Matsuo H. Solution NMR structure of the N-terminal domain of the human DEK protein. Protein science : a publication of the Protein Society. 2008 Feb;17(2):205–215.
Journal cover image

Published In

Protein science : a publication of the Protein Society

DOI

EISSN

1469-896X

ISSN

0961-8368

Publication Date

February 2008

Volume

17

Issue

2

Start / End Page

205 / 215

Related Subject Headings

  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Poly-ADP-Ribose Binding Proteins
  • Oncogene Proteins
  • Nuclear Magnetic Resonance, Biomolecular
  • Molecular Sequence Data
  • Humans
  • DNA-Binding Proteins