| Literature DB >> 10716989 |
P R Mittl1, C Deillon, D Sargent, N Liu, S Klauser, R M Thomas, B Gutte, M G Grütter.
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.Mesh:
Substances:
Year: 2000 PMID: 10716989 PMCID: PMC15968 DOI: 10.1073/pnas.97.6.2562
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205