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Structures of heterodimeric POZ domains of Miz1/BCL6 and Miz1/NAC1

DOI: 10.1107/S2053230X14023449 DOI Help
PMID: 25484205 PMID Help

Authors: Mark Stead (School of Biology, University of Leeds) , Stephanie Wright (School of Biology, University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 1591 - 1596

State: Published (Approved)
Published: December 2014

Abstract: The POZ domain is an evolutionarily conserved protein-protein interaction domain that is found in approximately 40 mammalian transcription factors. POZ domains mediate both homodimerization and the heteromeric interactions of different POZ-domain transcription factors with each other. Miz1 is a POZ-domain transcription factor that regulates cell-cycle arrest and DNA-damage responses. The activities of Miz1 are altered by its interaction with the POZ-domain transcriptional repressors BCL6 and NAC1, and these interactions have been implicated in tumourigenesis in B-cell lymphomas and in ovarian serous carcinomas that overexpress BCL6 and NAC1, respectively. A strategy for the purification of tethered POZ domains that form forced heterodimers is described, and crystal structures of the heterodimeric POZ domains of Miz1/BCL6 and of Miz1/NAC1 are reported. These structures will be relevant for the design of therapeutics that target POZ-domain interaction interfaces.

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 25/02/2015 10:00

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