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The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.

P R Mittl·C Deillon·D Sargent·N Liu·S Klauser·R M Thomas·B Gutte·M G Grütter
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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.

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Amino Acid SequenceCrystallography, X-RayDNA-Binding ProteinsEnhancer Elements, GeneticFungal ProteinsLeucine ZippersModels, MolecularMolecular Sequence DataPeptidesProtein ConformationProtein KinasesRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUltracentrifugationJournal ArticleResearch Support, Non-U.S. Gov't

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P R Mittl, C Deillon, D Sargent, N Liu, S Klauser, R M Thomas, B Gutte, M G Grütter. 2000-03-14. The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.. https://doi.org/10.1073/pnas.97.6.2562

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