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Structure of the wild-type human BCL6 POZ domain.

Authors :
Stead, Mark A.
Rosbrook, Gareth O.
Hadden, Jonathan M.
Trinh, Chi H.
Carr, Stephen B.
Wright, Stephanie C.
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