The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure
收藏PubMed Central2000-03-14 更新2026-04-25 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC15968/
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资源简介：
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 very stable, parallel four-helix bundle, which now lends itself to further structural and functional studies.
提供机构：
National Academy of Sciences
创建时间：
2000-03-14
