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-Å 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...
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| Yayımlandı: | Proc Natl Acad Sci U S A |
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| Asıl Yazarlar: | , , , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
National Academy of Sciences
2000
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC15968/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10716989/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.97.6.2562 |
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