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

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

The Journal of biological chemistry - 29 Sept 2000

Stevens K, Cirillo L, Zaret K S

Abstract excerpt

Winged helix transcription factors contain two polypeptide loops, or "wings," that make minor groove contacts with DNA from either side of a three-helix bundle that binds the DNA major groove. While wing 1 is stabilized by a beta-sheet, parameters that stabilize wing 2 are unknown. Herein we identify two bulky aromatic residues in wing 2 that stabilize the loop structure and, thereby, the entire protein's DNA...

Read the complete abstract on PubMed

Topics

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

Share to Evolution, Molecular
Share to Helix-Loop-Helix Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hepatocyte Nuclear Factor 3-alpha

Share to Mutagenesis, Site-Directed

Share to Nuclear Proteins

Share to Protein Structure, Tertiary

Share to Temperature

Share to Transcription, Genetic

Source

Identifiers

PMID: 10896667
DOI: 10.1074/jbc.M004891200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Creating temperature-sensitive winged helix transcription factors. Amino acids that stabilize the DNA binding domain of HNF3.PMID 10896667Read ↗

Structural Basis for DNA Recognition by FOXG1 and the Characterization of Disease-causing FOXG1 Mutations.Semantic proximity Read ↗

TF-MAPS: fast high-resolution functional and allosteric mapping of DNA-binding proteinsSemantic proximity Read ↗

Context-Dependent Gene Regulation by Homeodomain Transcription Factor Complexes Revealed by Shape-Readout Deficient Proteins.Semantic proximity Read ↗

The structural basis for forkhead box family specificity revealed by the crystal structure of human FOXN1 in complex with DNASemantic proximity Read ↗

An activity-specificity trade-off encoded in human transcription factors.Semantic proximity Read ↗

Structural bases for Nuclear Factor 1-X activation and DNA recognition. Prototypic insight into the NFI transcription factor familySemantic proximity Read ↗

Structural insights into human TFIIIC promoter recognitionSemantic proximity Read ↗

The Fen1 extrahelical 3'-flap pocket is conserved from archaea to human and regulates DNA substrate specificity.Semantic proximity Read ↗

A small conserved surface in SUMO is the critical structural determinant of its transcriptional inhibitory properties.Semantic proximity Read ↗

NF-Y binding to twin CCAAT boxes: role of Q-rich domains and histone fold helices.Semantic proximity Read ↗

Investigation of the β-sheet interactions between dHP1 chromodomain and histone 3.Semantic proximity Read ↗

Engineering a protein scaffold from a PHD finger.Semantic proximity Read ↗

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