Structure of a BCOR Corepressor Peptide in Complex with the BCL6 BTB Domain Dimer
Open accessAbstract
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.
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These molecules bind the BTB domain, which mediates BCL6 homodimerization and its interactions with co-repressor proteins.
“These molecules bind the Broad complex/Tramtrack/Bric-a-brac (BTB) domain, which mediates BCL6 homodimerization and its interactions with co-repressor proteins22.”
From Small-molecule-induced polymerization triggers degradation of BCL6 (2020) · cites this paper as [22]
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References 24 · Cited by 168
- Authors
- Ghetu, A. F., Corcoran, C. M., Cerchietti, L., Bardwell, V. J., Melnick, A., & Privé, G. G.
- Affiliations
- University of Minnesota (US)
- Albert Einstein College of Medicine (US)
- University of Toronto (CA)
- Corresponding author
- Privé, Gilbert G.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-02
- Volume
- 29
- Issue
- 3
- Pages
- 384-391
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC2665293
- OpenAlex
- W2065292885
- Cited by
- 168
- References
- 24
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 9 · 2023: 7 · 2022: 19 · 2021: 13 · 2020: 14 · 2019: 7 · 2018: 8 · 2017: 13 · 2016: 10 · 2015: 6 · 2014: 11 · 2013: 5 · 2012: 5
- FWCI
- 3.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Canadian Institutes of Health Research
- National Cancer Institute (R01CA071540, R01 CA71540, R01CA104348)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- BCOR, BCL6, BTB domain, corepressors, SMRT, NCoR, protein-protein interaction, crystal structure, competitive binding, transcriptional repression, lymphoma
- MeSH terms
- Amino Acid Sequence, Binding Sites, Histidine, Models, Chemical, Models, Molecular, Molecular Sequence Data, Mutation, Peptides, Protein Binding, Protein Conformation, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Repressor Proteins, Thioredoxins, Sequence Alignment, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization, Amino Acid Motifs, Proto-Oncogene Proteins c-bcl-6
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