Literature DB >> 19052359

Structure of the wild-type human BCL6 POZ domain.

Mark A Stead1, Gareth O Rosbrook, Jonathan M Hadden, Chi H Trinh, Stephen B Carr, Stephanie C Wright.   

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.

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Year:  2008        PMID： 19052359      PMCID： PMC2593701          DOI： 10.1107/S1744309108036063

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  34 in total

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  4 in total

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Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-11-14       Impact factor: 1.056

3.  Structural analysis of the PATZ1 BTB domain homodimer.

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Journal:  Acta Crystallogr D Struct Biol       Date:  2020-05-29       Impact factor: 7.652

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Journal:  PLoS One       Date:  2013-10-11       Impact factor: 3.240
  4 in total

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