title: The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
abstract: The question of whether a protein whose natural sequence is inverted adopts a stable fold is still under debate. We have determined the 2. 1-A crystal structure of the retro-GCN4 leucine zipper. In contrast to the two-stranded helical coiled-coil GCN4 leucine zipper, the retro-leucine zipper formed a very stable, parallel four-helix bundle, which now lends itself to further structural and functional studies.
authors.affiliation: Biochemisches Institut der Universität Zürich, Winterthurer Strasse 190, CH-8057 Zürich, Switzerland.
authors.forename: P R
authors.initials: PR
authors.lastname: Mittl
authors.forename: C
authors.initials: C
authors.lastname: Deillon
authors.forename: D
authors.initials: D
authors.lastname: Sargent
authors.forename: N
authors.initials: N
authors.lastname: Liu
authors.forename: S
authors.initials: S
authors.lastname: Klauser
authors.forename: R M
authors.initials: RM
authors.lastname: Thomas
authors.forename: B
authors.initials: B
authors.lastname: Gutte
authors.forename: M G
authors.initials: MG
authors.lastname: Grütter
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D004742:Enhancer Elements, Genetic; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D016350:Leucine Zippers; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D014461:Ultracentrifugation
chemical_list: D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D010455:Peptides; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases