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An engineered allosteric switch in leucine-zipper oligomerization

Nature Structural Biology volume 3, pages 510–515 (1996)Cite this article

An Erratum to this article was published on 01 July 1996

Abstract

Controversy remains about the role of core side-chain packing in specifying protein structure. To investigate the influence of core packing on the oligomeric structure of a coiled coil, we engineered a GCN4 leucine zipper mutant that switches from two to three strands upon binding the hydrophobic ligands cyclohexane and benzene. In solution these ligands increased the apparent thermal stability and the oligomerization order of the mutant leucine zipper. The crystal structure of the peptide–benzene complex shows a single benzene molecule bound at the engineered site in the core of the trimer. These results indicate that coiled coils are well-suited to function as molecular switches and emphasize that core packing is an important determinant of oligomerization specificity.

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Authors and Affiliations

  1. Department of Molecular and Cell Biology, 229 Stanley Hall, University of California, Berkeley, California, 94720-3206, USA

    Lino Gonzalez Jr. & Tom Alber

  2. Department of Physics, University of California, Berkeley, California, 94720, USA

    Joseph J. Plecs

Authors
  1. Lino Gonzalez Jr.
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  2. Joseph J. Plecs
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  3. Tom Alber
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Gonzalez, L., Plecs, J. & Alber, T. An engineered allosteric switch in leucine-zipper oligomerization. Nat Struct Mol Biol 3, 510–515 (1996). https://doi.org/10.1038/nsb0696-510

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