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

Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior.

Genes & development - 15 Aug 2003

LaRonde-LeBlanc Nicole A, Wolberger Cynthia

Abstract excerpt

The HOX/HOM superfamily of homeodomain proteins controls cell fate and segmental embryonic patterning by a mechanism that is conserved in all metazoans. The linear arrangement of the Hox genes on the chromosome correlates with the spatial distribution of HOX protein expression along the anterior-posterior axis of the embryo. Most HOX proteins bind DNA cooperatively with members of the PBC family of TALE-type...

Read the complete abstract on PubMed

Topics

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

Share to Conserved Sequence
Share to Drosophila
Share to Homeodomain Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nucleic Acid Conformation

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to Proto-Oncogene Proteins

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 12923056
DOI: 10.1101/gad.1103303
PMCID: PMC196259

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

Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior.PMID 12923056Read ↗

Loss of function but no gain of function caused by amino acid substitutions in the hexapeptide of Hoxa1 in vivo.Semantic proximity Read ↗

Definition of the transcriptional activation domains of three human HOX proteins depends on the DNA-binding context.Semantic proximity Read ↗

Functional characterisation of a HOX/PBX transcriptional complexSemantic proximity Read ↗

In vivo mutagenesis of the Hoxb8 hexapeptide domain leads to dominant homeotic transformations that mimic the loss-of-function mutations in genes of the Hoxb cluster.Semantic proximity Read ↗

Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax.Semantic proximity Read ↗

Sequences outside the homeodomain of bicoid are required for protein-protein interaction.Semantic proximity Read ↗

Switching the in vivo specificity of a minimal Hox-responsive element.Semantic proximity Read ↗

Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility.Semantic proximity Read ↗

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

Hox/Pbx and Brn binding sites mediate Pax3 expression in vitro and in vivo.Semantic proximity Read ↗

Yin Yang 1 physically interacts with Hoxa11 and represses Hoxa11-dependent transcription.Semantic proximity Read ↗

A conserved motif N-terminal to the DNA-binding domains of myogenic bHLH transcription factors mediates cooperative DNA binding with pbx-Meis1/Prep1.Semantic proximity Read ↗

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