The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
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.
Mittl
P R
PR
Biochemisches Institut der Universität Zürich, Winterthurer Strasse 190, CH-8057 Zürich, Switzerland.
Deillon
C
C
Sargent
D
D
Liu
N
N
Klauser
S
S
Thomas
R M
RM
Gutte
B
B
Grütter
M G
MG
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
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D010455:Peptides; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases