4U2M
Crystal structure of a complex of the Miz1- and BCL6 POZ domains.
Summary for 4U2M
Entry DOI | 10.2210/pdb4u2m/pdb |
Related | 4u2n |
Descriptor | Zinc finger and BTB domain-containing protein 17,B-cell lymphoma 6 protein (2 entities in total) |
Functional Keywords | poz domain, btb domain, transcription |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus : P41182 |
Total number of polymer chains | 4 |
Total formula weight | 113310.59 |
Authors | Stead, M.A.,Wright, S.C. (deposition date: 2014-07-17, release date: 2014-12-10, Last modification date: 2024-05-08) |
Primary citation | Stead, M.A.,Wright, S.C. Structures of heterodimeric POZ domains of Miz1/BCL6 and Miz1/NAC1. Acta Crystallogr.,Sect.F, 70:1591-1596, 2014 Cited by PubMed 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. PubMed: 25484205DOI: 10.1107/S2053230X14023449 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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