3DM1

Crystal structure of the complex of human chromobox homolog 3 (CBX3) with peptide

Summary for 3DM1

• Entry DOI: 10.2210/pdb3dm1/pdb
• Descriptor: Chromobox protein homolog 3, Histone-lysine N-methyltransferase, H3 lysine-9 specific 3 (3 entities in total)
• Functional Keywords: chromobox homolog 3, structural genomics, structural genomics consortium, sgc, chromatin regulator, nucleus, phosphoprotein, repressor, transcription, transcription regulation
• Biological source: Homo sapiens; More
• Cellular location: Nucleus : Q13185 Q96KQ7
• Total number of polymer chains: 8
• Total formula weight: 33198.05

Authors

Amaya, M.F.,Ravichandran, M.,Loppnau, P.,Kozieradzki, I.,Edwards, A.M.,Arrowsmith, C.H.,Weigelt, J.,Bountra, C.,Bochkarev, A.,Min, J.,Ouyang, H.,Structural Genomics Consortium (SGC) (deposition date: 2008-06-30, release date: 2008-08-19, Last modification date: 2025-03-26)

Primary citation

Ruan, J.,Ouyang, H.,Amaya, M.F.,Ravichandran, M.,Loppnau, P.,Min, J.,Zang, J.
Structural basis of the chromodomain of Cbx3 bound to methylated peptides from histone h1 and G9a.
Plos One, 7:e35376-e35376, 2012

PubMed Abstract: HP1 proteins are highly conserved heterochromatin proteins, which have been identified to be structural adapters assembling a variety of macromolecular complexes involved in regulation of gene expression, chromatin remodeling and heterochromatin formation. Much evidence shows that HP1 proteins interact with numerous proteins including methylated histones, histone methyltransferases and so on. Cbx3 is one of the paralogues of HP1 proteins, which has been reported to specifically recognize trimethylated histone H3K9 mark, and a consensus binding motif has been defined for the Cbx3 chromodomain.

PubMed: 22514736
DOI: 10.1371/journal.pone.0035376

Experimental method

X-RAY DIFFRACTION (2.4 Å)