Two pairs of oppositely charged amino acids from Jun and Fos confer heterodimerization to GCN4 leucine zipper.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. Interactions of coiled coils in transcription factors: where is the specificity?
2. Dimers, leucine zippers and DNA-binding domains
3. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex
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1. Oligomerization properties of GCN4 leucine zipper e and g position mutants;Protein Science;2008-12-31
2. Selectional and Mutational Scope of Peptides Sequestering the Jun–Fos Coiled-Coil Domain;Journal of Molecular Biology;2008-08
3. Structural Basis for the Conformational Integrity of the Arabidopsis thaliana HY5 Leucine Zipper Homodimer;Journal of Biological Chemistry;2007-04
4. Semirational design of Jun-Fos coiled coils with increased affinity: Universal implications for leucine zipper prediction and design;Proceedings of the National Academy of Sciences;2006-06-05
5. Dimerization Specificity of Adult and Neonatal Chicken Skeletal Muscle Myosin Heavy Chain Rods;Biochemistry;2006-03-28
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