Journal of Biomolecular NMR

, Volume 60, Issue 2–3, pp 189–195 | Cite as

Solution structure of the free Zα domain of human DLM-1 (ZBP1/DAI), a Z-DNA binding domain

  • Yunhuang Yang
  • Theresa A. Ramelot
  • Hsiau-Wei Lee
  • Rong Xiao
  • John K. Everett
  • Gaetano T. Montelione
  • James H. Prestegard
  • Michael A. Kennedy
NMR Structure Note

Biological context

The protein DLM-1 (also called Z-DNA binding protein 1, ZBP1) is the product of the dlm-1 gene. The dlm-1 gene was initially isolated and identified using the RNA differential display technique where they found that it was highly up-regulated in the peritoneal lining tissue of mice bearing nearby ovarian tumors and in activated macrophages (Fu et al. 1999). DLM-1 was proposed to play a role in host defense against tumors, although its precise function was unknown (Fu et al. 1999). In 2001, the N-terminal domain of mouse DLM-1 (ZαDLM-1) was co-crystallized with left-handed Z-DNA (PDB ID 1J75) (Schwartz et al. 2001). The complex structure revealed that ZαDLM-1 is structurally similar to the Zα domain of double-stranded RNA adenosine deaminase ADAR1 (ZαADAR1), the first crystal structure of a protein bound to left-handed Z-DNA (PDB ID 1QBJ) (Schwartz et al. 1999), although they only share about 35 % amino acid sequence identity (Schade et al. 1999; Schwartz et al. 1999)...


Residual Dipolar Coupling Phosphodiester Backbone Dihedral Angle Restraint NOESY Peak List Hydrogen Bond Restraint 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



This work was supported by the National Institute of General Medical Sciences; Protein Structure Initiative-Biology Program; Grant Numbers: U54-GM074958 and U54-GM094597. We thank K. Hamilton, E. Kohan, D. Wang, and T. Acton at the Rutgers’ protein production facility for technical support. All NMR data collection, except RDCs collected at the University of Georgia, was conducted at the Ohio Biomedicine Center of Excellence for Structural Biology and Metabonomics at Miami University.


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Copyright information

© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Yunhuang Yang
    • 1
  • Theresa A. Ramelot
    • 1
  • Hsiau-Wei Lee
    • 2
  • Rong Xiao
    • 3
  • John K. Everett
    • 3
  • Gaetano T. Montelione
    • 3
    • 4
  • James H. Prestegard
    • 2
  • Michael A. Kennedy
    • 1
  1. 1.Department of Chemistry and Biochemistry, and the Northeast Structural Genomics ConsortiumMiami UniversityOxfordUSA
  2. 2.Complex Carbohydrate Research Center, and the Northeast Structural Genomics ConsortiumUniversity of GeorgiaAthensUSA
  3. 3.Department of Molecular Biology and Biochemistry, and the Northeast Structural Genomics Consortium, Center for Advanced Biotechnology and MedicineRutgers, The State University of New JerseyPiscatawayUSA
  4. 4.Department of Biochemistry, Robert Wood Johnson Medical SchoolUniversity of Medicine and Dentistry of New JerseyPiscatawayUSA

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