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Buried polar residues and structural specificity in the GCN4 leucine zipper

Nature Structural Biology volume 3, pages 1011–1018 (1996)Cite this article

Abstract

A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gin and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn16Lys mutant formed exclusively dimers. In contrast. Gin 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gin 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment.

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Author information

Author notes

  1. Derek N. Woolfson

    Present address: School of Biological Sciences, University of Sussex, Palmer, BN1 9QG, UK

  2. Lino Gonzalez and Derek N. Woolfson: Contributed equally to this work

Authors and Affiliations

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

    Tom Alber

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  1. Lino Gonzalez Jr.
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  2. Derek N. Woolfson
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  3. Tom Alber
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Gonzalez, L., Woolfson, D. & Alber, T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nat Struct Mol Biol 3, 1011–1018 (1996). https://doi.org/10.1038/nsb1296-1011

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