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Structure of the wild-type human BCL6 POZ domain.
- Source :
- Acta Crystallographica: Section F (Wiley-Blackwell); Dec2008, Vol. 64 Issue 12, p1101-1104, 4p
- Publication Year :
- 2008
-
Abstract
- BCL6 is a transcriptional repressor that is overexpressed in diffuse large B-cell lymphoma and follicular lymphoma. The N-terminal POZ domain of BCL6 interacts with transcriptional corepressors and targeting these associations is a promising therapeutic strategy. Previous structural studies of the BCL6 POZ domain have used a mutant form because of the low solubility of the wild-type recombinant protein. A method for the purification and crystallization of the wild-type BCL6 POZ domain is described and the crystal structure to 2.1 Å resolution is reported. This will be relevant for the design of therapeutics that target BCL6 POZ-domain interaction interfaces. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 64
- Issue :
- 12
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812069
- Full Text :
- https://doi.org/10.1107/S1744309108036063