title: Structure of the leucine zipper.
abstract: In the basic-region leucine-zipper domain, flexible DNA-binding arms are juxtaposed by a two-stranded, parallel coiled-coil motif called the leucine zipper. Genetic, physical and structural studies of the leucine zipper identify interactions that help determine the stability and specificity of dimerization and DNA binding.
authors.affiliation: Department of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132.
authors.forename: T
authors.initials: T
authors.lastname: Alber
mesh_terms: D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry*; D016350:Leucine Zippers / Q000235:genetics / Q000502:physiology; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D004268:DNA-Binding Proteins