Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.

doi:10.1002/pro.5560020701

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Article

Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.

Protein science : a publication of the Protein Society - 1 Jul 1993

Hu J C, Newell N E, Tidor B, Sauer R T

Abstract excerpt

Combinatorial mutagenesis with an alphabet limited to alanine, glutamic acid, lysine, and threonine was used to probe the role of interactions involving surface residues in stabilizing a short alpha-helical coiled coil. The residues at eight e and g positions in the leucine zipper of the Saccharomyces cerevisiae transcription factor GCN4 were randomized to these four residues in a lambda repressor-leucine zipper...

Topics

Amino Acid Sequence
Base Sequence
DNA-Binding Proteins
Escherichia coli
Fungal Proteins
Genetic Variation
Glutamates
Glutamic Acid
Glycine
Leucine Zippers
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Protein Conformation

Protein Kinases

Protein Structure, Secondary

Recombinant Fusion Proteins

Repressor Proteins

Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 8102921
DOI: 10.1002/pro.5560020701
PMCID: PMC2142419

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8102921-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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