Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins

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. and Behlke, J. and Lowenhaupt, K. and 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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