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

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.

SUBMITTER: Mittl PR 

PROVIDER: S-EPMC15968 | biostudies-literature | 2000 Mar

REPOSITORIES: biostudies-literature

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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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