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Structure of the wild-type human BCL6 POZ domain.


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 A resolution is reported. This will be relevant for the design of therapeutics that target BCL6 POZ-domain interaction interfaces.

SUBMITTER: Stead MA 

PROVIDER: S-EPMC2593701 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Structure of the wild-type human BCL6 POZ domain.

Stead Mark A MA   Rosbrook Gareth O GO   Hadden Jonathan M JM   Trinh Chi H CH   Carr Stephen B SB   Wright Stephanie C SC  

Acta crystallographica. Section F, Structural biology and crystallization communications 20081128 Pt 12


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 describ  ...[more]

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