Structure of the DLM-1–Z-DNA complex reveals a conserved family of Z-DNA-binding proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-09

AUTHORS

Thomas Schwartz, Joachim Behlke, Ky Lowenhaupt, Udo Heinemann, Alexander Rich

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 Å 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. More... »

PAGES

761-765

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0901-761

DOI

http://dx.doi.org/10.1038/nsb0901-761

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025587071

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11524677


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