| First Author | Schwartz T | Year | 2001 |
| Journal | Nat Struct Biol | Volume | 8 |
| Issue | 9 | Pages | 761-5 |
| PubMed ID | 11524677 | Mgi Jnum | J:74605 |
| Mgi Id | MGI:2158862 | Doi | 10.1038/nsb0901-761 |
| Citation | Schwartz T, et al. (2001) Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins. Nat Struct Biol 8(9):761-5 |
| abstractText | The first crystal structure of a protein, the Z alpha 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 Z alpha(ADAR). Here we report the crystal structure of this DLM-1 domain bound to left-handed Z-DNA at 1.85 A 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. |
