Stead, MA, Rosbrook, GO, Hadden, JM et al. (3 more authors) (2008) Structure of the wild-type human BCL6 POZ domain. Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 64 (12). 1101 - 1104. ISSN 1744-3091
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © International Union of Crystallography. Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | BCL6; POZ domains; BTB; Miz-1 |
Dates: |
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Institution: | The University of Leeds |
Depositing User: | Symplectic Publications |
Date Deposited: | 11 Jul 2014 11:52 |
Last Modified: | 11 Jul 2014 11:59 |
Published Version: | http://dx.doi.org/10.1107/S1744309108036063 |
Status: | Published |
Publisher: | International Union of Crystallography |
Refereed: | Yes |
Identification Number: | 10.1107/S1744309108036063 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:79621 |