Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions.

Science (New York, N.Y.) - 7 Dec 1990

Hu J C, O'Shea E K, Kim P S, Sauer R T

Abstract excerpt

A genetic system was developed in Escherichia coli to study leucine zippers with the amino-terminal domain of bacteriophage lambda repressor as a reporter for dimerization. This system was used to analyze the importance of the amino acid side chains at eight positions that form the hydrophobic interface of the leucine zipper dimer from the yeast transcriptional activator, GCN4. When single amino acid...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to DNA-Binding Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Genetic Variation

Share to Molecular Sequence Data

Share to Phenotype

Share to Transcription Factors

Source

Identifiers

PMID: 2147779
DOI: 10.1126/science.2147779

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions.PMID 2147779Read ↗

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

Buried asparagines determine the dimerization specificities of leucine zipper mutants.Semantic proximity Read ↗

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.Semantic proximity Read ↗

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

An engineered allosteric switch in leucine-zipper oligomerization.Semantic proximity Read ↗

A parallel coiled-coil tetramer with offset helices.Semantic proximity Read ↗

De Novo Designed Protein-Interaction Modules for In-Cell ApplicationsSemantic proximity Read ↗

Prediction of quaternary structure of coiled coils. Application to mutants of the GCN4 leucine zipper.Semantic proximity Read ↗

Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.Semantic proximity Read ↗

Buried polar residues and structural specificity in the GCN4 leucine zipper.Semantic proximity Read ↗

The role of internal packing interactions in determining the structure and stability of a protein.Semantic proximity Read ↗

An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.