Solution structure of the free Zα domain of human DLM-1 (ZBP1/DAI), a Z-DNA binding domain
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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)...
KeywordsResidual Dipolar Coupling Phosphodiester Backbone Dihedral Angle Restraint NOESY Peak List Hydrogen Bond Restraint
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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