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

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...

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Podrobná bibliografie

Vydáno v:	Proc Natl Acad Sci U S A
Hlavní autoři:	Mittl, Peer R. E., Deillon, Christine, Sargent, David, Liu, Niankun, Klauser, Stephan, Thomas, Richard M., Gutte, Bernd, Grütter, Markus G.
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	National Academy of Sciences 2000
Témata:	Biological Sciences
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC15968/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10716989/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.97.6.2562
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