期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 97, 期 6, 页码 2562-2566出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.97.6.2562
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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-Angstrom 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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