4AFL

The crystal structure of the ING4 dimerization domain reveals the functional organization of the ING family of chromatin binding proteins.

Summary for 4AFL

• Entry DOI: 10.2210/pdb4afl/pdb
• Related: 2VNF
• Descriptor: INHIBITOR OF GROWTH PROTEIN 4 (2 entities in total)
• Functional Keywords: cell cycle, tumour suppressor, chromatin remodelling
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus: Q9UNL4
• Total number of polymer chains: 6
• Total formula weight: 74407.46

Authors

Culurgioni, S.,Munoz, I.G.,Moreno, A.,Palacios, A.,Villate, M.,Palmero, I.,Montoya, G.,Blanco, F.J. (deposition date: 2012-01-19, release date: 2012-02-22, Last modification date: 2024-10-23)

Primary citation

Culurgioni, S.,Munoz, I.G.,Moreno, A.,Palacios, A.,Villate, M.,Palmero, I.,Montoya, G.,Blanco, F.J.
Crystal Structure of Inhibitor of Growth 4 (Ing4) Dimerization Domain Reveals Functional Organization of Ing Family of Chromatin-Binding Proteins.
J.Biol.Chem., 287:10876-, 2012

PubMed Abstract: 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, which shows an antiparallel coiled-coil homodimer with each protomer folded into a helix-loop-helix structure. This arrangement suggests that ING4 can bind simultaneously two histone tails on the same or different nucleosomes. Dimerization has a direct impact on ING4 tumor suppressor activity because monomeric mutants lose the ability to induce apoptosis after genotoxic stress. Homology modeling based on the ING4 structure suggests that other ING dimers may also exist.

PubMed: 22334692
DOI: 10.1074/JBC.M111.330001

Experimental method

X-RAY DIFFRACTION (2.275 Å)