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| Item Type: | Article |
|---|---|
| Title: | Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins |
| Creators Name: | Schwartz, T., Behlke, J., Lowenhaupt, K., Heineman, U. and Rich, A. |
| Abstract: | The first crystal structure of a protein, the Zα high affinity binding domain of the RNA editing enzyme ADAR1, bound to left-handed Z-DNA was recently described. The essential set of residues determined from this structure to be critical for Z-DNA recognition was used to search the database for other proteins with the potential for Z-DNA binding. We found that the tumor-associated protein DLM-1 contains a domain with remarkable sequence similarities to ZαADAR. Here we report the crystal structure of this DLM-1 domain bound to left-handed Z-DNA at 1.85 {angstrom} resolution. Comparison of Z-DNA binding by DLM-1 and ADAR1 reveals a common structure-specific recognition core within the binding domain. However, the domains differ in certain residues peripheral to the protein-DNA interface. These structures reveal a general mechanism of Z-DNA recognition, suggesting the existence of a family of winged-helix proteins sharing a common Z-DNA binding motif. |
| Keywords: | Adenosine Deaminase, Amino Acid Sequence, Conserved Sequence, DNA, DNA-Binding Proteins, Glycoproteins, Molecular Models, Molecular Sequence Data, Nucleic Acid Conformation, Protein Conformation, Sequence Alignment, Tertiary Protein Structure, Ultracentrifugation, X-Ray Crystallography, Animals, Mice |
| Source: | Nature Structural Biology |
| ISSN: | 1072-8368 |
| Publisher: | Nature America Inc |
| Volume: | 8 |
| Number: | 9 |
| Page Range: | 761-765 |
| Date: | 1 January 2001 |
| PubMed: | View item in PubMed |
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