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Structure of the wild-type human BCL6 POZ domain

DOI: 10.1107/S1744309108036063 DOI Help
PMID: 19052359 PMID Help

Authors: Mark Stead (Institute of Molecular and Cellular Biology, University of Leeds) , Gareth Rosbrook (Institute of Molecular and Cellular Biology, University of Leeds) , Jonathan Hadden (Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds) , Chi Trinh (Institute of Molecular and Cellular Biology, University of Leeds) , Stephen Carr (Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds) , Stephanie Wright (Institute of Molecular and Cellular Biology, University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 , PAGES 1101 - 1104

State: Published (Approved)
Published: December 2008
Diamond Proposal Number(s): 302

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.

Journal Keywords: Cloning; Molecular; DNA-Binding; Humans; Models; Molecular; Protein; Tertiary; Recombinant Proteins

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I04-Macromolecular Crystallography

Added On: 17/08/2011 12:41

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