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Article

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.

Science (New York, N.Y.) - 26 Nov 1993

Harbury P B, Zhang T, Kim P S, Alber T

Abstract excerpt

Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer...

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Identifiers

PMID: 8248779
DOI: 10.1126/science.8248779

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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