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Article

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

The Journal of biological chemistry - 30 Mar 2012

Culurgioni Simone, Muñoz Inés G, Moreno Alberto, Palacios Alicia, Villate Maider, Palmero Ignacio, Montoya Guillermo, Blanco Francisco J

Abstract excerpt

The protein ING4 binds to histone H3 trimethylated at Lys-4 (H3K4me3) through its C-terminal plant homeodomain, thus recruiting the HBO1 histone acetyltransferase complex to target promoters. The structure of the plant homeodomain finger bound to an H3K4me3 peptide has been described, as well as the disorder and flexibility in the ING4 central region. We report the crystal structure of the ING4 N-terminal domain,...

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Topics

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Share to Cell Cycle Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Histone Acetyltransferases

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Share to Mutagenesis, Site-Directed

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Source

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Identifiers

PMID: 22334692
DOI: 10.1074/jbc.M111.330001
PMCID: PMC3322854

Genes

ING4

Provenance

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Crystal structure of inhibitor of growth 4 (ING4) dimerization domain reveals functional organization of ING family of chromatin-binding proteins.PMID 22334692Read ↗

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