Open AccessStructure of the wild‐type human BCL6 POZ domain
Author(s) -
Stead Mark A.,
Rosbrook Gareth O.,
Hadden Jonathan M.,
Trinh Chi H.,
Carr Stephen B.,
Wright Stephanie C.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108036063
Subject(s) - domain (mathematical analysis) , materials science , mathematics , mathematical analysis
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.