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

Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2.

Nature - 6 Jul 2006

Peña Pedro V, Davrazou Foteini, Shi Xiaobing, Walter Kay L, Verkhusha Vladislav V, Gozani Or, Zhao Rui, Kutateladze Tatiana G

Abstract excerpt

Covalent modifications of histone tails have a key role in regulating chromatin structure and controlling transcriptional activity. In eukaryotes, histone H3 trimethylated at lysine 4 (H3K4me3) is associated with active chromatin and gene expression. We recently found that plant homeodomain (PHD) finger of tumour suppressor ING2 (inhibitor of growth 2) binds H3K4me3 and represents a new family of modules that...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Conserved Sequence

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

Share to Crystallography, X-Ray

Share to Histones

Share to Hydrogen Bonding

Share to Lysine

Share to Methylation

Share to Tumor Suppressor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16728977
DOI: 10.1038/nature04814
PMCID: PMC3190580

Genes

ING2

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

Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2.PMID 16728977Read ↗

Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins.Semantic proximity Read ↗

Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor.Semantic proximity Read ↗

Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.Semantic proximity Read ↗

Structural basis of molecular recognition of helical histone H3 tail by PHD finger domains.Semantic proximity Read ↗

Function of the ING family of PHD proteins in cancer.Semantic proximity Read ↗

Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53.Semantic proximity Read ↗

A common mechanism for mitotic inactivation of C2H2 zinc finger DNA-binding domains.Semantic proximity Read ↗

Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.Semantic proximity Read ↗

A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36.Semantic proximity Read ↗

Allosteric activation dictates PRC2 activity independent of its recruitment to chromatinSemantic proximity Read ↗

Structure and site-specific recognition of histone H3 by the PHD finger of human autoimmune regulator.Semantic proximity Read ↗

ING2 recruits histone methyltransferase activity with methylation site specificity distinct from histone H3 lysines 4 and 9.Semantic proximity Read ↗

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