3BIM

Crystal structure of the BCL6 BTB domain dimer in complex with the BCOR BBD corepressor peptide

Summary for 3BIM

• Entry DOI: 10.2210/pdb3bim/pdb
• Descriptor: B-cell lymphoma 6 protein, BCL-6 corepressor (3 entities in total)
• Functional Keywords: protein-peptide compex, activator, chromosomal rearrangement, dna-binding, metal-binding, nucleus, phosphoprotein, polymorphism, proto-oncogene, repressor, transcription, transcription regulation, zinc, zinc-finger, alternative splicing, ank repeat, chromatin regulator, disease mutation, transcription repressor
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : P41182 Q6W2J9
• Total number of polymer chains: 16
• Total formula weight: 131903.61

Authors

Prive, G.G.,Ghetu, A.F. (deposition date: 2007-11-30, release date: 2008-01-08, Last modification date: 2023-08-30)

Primary citation

Ghetu, A.F.,Corcoran, C.M.,Cerchietti, L.,Bardwell, V.J.,Melnick, A.,Prive, G.G.
Structure of a BCOR corepressor peptide in complex with the BCL6 BTB domain dimer.
Mol.Cell, 29:384-391, 2008

PubMed Abstract: The transcriptional corepressors BCOR, SMRT, and NCoR are known to bind competitively to the BCL6 BTB domain despite the fact that BCOR has no detectable sequence similarity to the other two corepressors. We have identified a 17 residue motif from BCOR that binds directly to the BCL6 BTB domain and determined the crystal structure of the complex to a resolution of 2.6 A. Remarkably, the BCOR BCL6 binding domain (BCOR(BBD)) peptide binds in the same BCL6 binding site as the SMRT(BBD) peptide despite the lack of any significant sequence similarity between the two peptides. Mutations of critical BCOR(BBD) residues cause the disruption of the BCL6 corepression activities of BCOR, and a BCOR(BBD) peptide blocks BCL6-mediated transcriptional repression and kills lymphoma cells.

PubMed: 18280243
DOI: 10.1016/j.molcel.2007.12.026

Experimental method

X-RAY DIFFRACTION (2.6 Å)