A Novel DNA Binding Mechanism for maf Basic Region-Leucine Zipper Factors Inferred from a MafA–DNA Complex Structure and Binding Specificities
Author:
Affiliation:
1. Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, United States
2. Z&W Electronics, 500 North Rainbow Boulevard, Suite 300A, Las Vegas, Nevada 89107, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi301248j
Reference55 articles.
1. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex
2. Altered protein conformation on DNA binding by Fos and Jun
3. Folding transition in the DMA-binding domain of GCN4 on specific binding to DNA
4. Solution structure of the DNA-binding domain of MafG
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