The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
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ABSTRACT:
SUBMITTER: Mittl PR
PROVIDER: S-EPMC15968 | biostudies-literature | 2000 Mar
REPOSITORIES: biostudies-literature
Publications
The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.
Mittl P R PR Deillon C C Sargent D D Liu N N Klauser S S Thomas R M RM Gutte B B Grütter M G MG
Proceedings of the National Academy of Sciences of the United States of America 20000301 6
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. ...[more]
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