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

The SKN-1 amino-terminal arm is a DNA specificity segment.

Molecular and cellular biology - 1 Apr 1999

Kophengnavong T, Carroll A S, Blackwell T K

Abstract excerpt

The Caenorhabditis elegans SKN-1 protein binds DNA through a basic region like those of bZIP proteins and through a flexible amino-terminal arm segment similar to those with which numerous helix-turn-helix proteins bind to bases in the minor groove. A recent X-ray crystallographic structure suggests that the SKN-1 amino-terminal arm provides only nonspecific DNA binding. In this study, however, we demonstrate...

Read the complete abstract on PubMed

Topics

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

Share to Adenine
Share to Caenorhabditis elegans
Share to Caenorhabditis elegans Proteins

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

Share to DNA Probes

Share to Helminth Proteins

Share to Nucleic Acid Conformation

Share to Sequence Deletion

Share to Thymine

Source

Open in PubMed Open full text

Identifiers

PMID: 10082571
DOI: 10.1128/MCB.19.4.3039
PMCID: PMC84098

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

The SKN-1 amino-terminal arm is a DNA specificity segment.PMID 10082571Read ↗

Multiple amino acids determine the DNA binding specificity of the Msx-1 homeodomain.Semantic proximity Read ↗

Regulation of ISWI involves inhibitory modules antagonized by nucleosomal epitopes.Semantic proximity Read ↗

Functional specificity of a Hox protein mediated by the recognition of minor groove structure.Semantic proximity Read ↗

The ancillary N-terminal region of the yeast AP-1 transcription factor Yap8 contributes to its DNA binding specificity.Semantic proximity Read ↗

Arginine-rich regions mediate the RNA binding and regulatory activities of the protein encoded by the Drosophila melanogaster suppressor of sable gene.Semantic proximity Read ↗

Substitution of DNA-contacting amino acids with functional variants in the Gata-1 zinc finger: a structurally and phylogenetically guided mutagenesis.Semantic proximity Read ↗

Creating temperature-sensitive winged helix transcription factors. Amino acids that stabilize the DNA binding domain of HNF3.Semantic proximity Read ↗

The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity.Semantic proximity Read ↗

Influence of amino acid numbers between two ligand cysteines of zinc finger proteins on affinity and specificity of DNA binding.Semantic proximity Read ↗

Mutations in the bZIP domain of yeast GCN4 that alter DNA-binding specificity.Semantic proximity Read ↗

In vivo analysis of scaffold-associated regions in Drosophila: a synthetic high-affinity SAR binding protein suppresses position effect variegation.Semantic proximity Read ↗

The degree of variation in DNA sequence recognition among four Drosophila homeotic proteins.Semantic proximity Read ↗

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