期刊
MOLECULAR CELL
卷 29, 期 3, 页码 384-391出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.12.026
关键词
-
资金
- NCI NIH HHS [R01 CA071540, R01 CA71540, R01 CA104348-05, R01 CA104348] Funding Source: Medline
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 angstrom. Remarkably, the BCOR BCL6 binding domain (BCORBBD) peptide binds in the same BCL6 binding site as the SMRTBBD peptide despite the lack of any significant sequence similarity between the two peptides. Mutations of critical BCORBBD residues cause the disruption of the BCL6 corepression activities of BCOR, and a BCORBBD peptide blocks BCL6-mediated transcriptional repression and kills lymphoma cells.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据