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Self-assembly of coiled-coil tetramers in the 1.40 Å structure of a leucine-zipper mutant
The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-typ...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
2007
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2203300/ https://ncbi.nlm.nih.gov/pubmed/17189475 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.062590807 |
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