2Q81

Crystal Structure of the Miz-1 BTB/POZ domain

Summary for 2Q81

• Entry DOI: 10.2210/pdb2q81/pdb
• Descriptor: Miz-1 protein, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: btb/poz domain, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q13105
• Total number of polymer chains: 4
• Total formula weight: 52478.24

Authors

Stead, M.A.,Trinh, C.H.,Garnett, J.A.,Carr, S.B.,Edwards, T.A.,Wright, S.C. (deposition date: 2007-06-08, release date: 2007-11-06, Last modification date: 2023-08-30)

Primary citation

Stead, M.A.,Trinh, C.H.,Garnett, J.A.,Carr, S.B.,Baron, A.J.,Edwards, T.A.,Wright, S.C.
A Beta-Sheet Interaction Interface Directs the Tetramerisation of the Miz-1 POZ Domain
J.Mol.Biol., 373:820-826, 2007

PubMed Abstract: The POZ/BTB domain is an evolutionarily conserved motif found in approximately 40 zinc-finger transcription factors (POZ-ZF factors). Several POZ-ZF factors are implicated in human cancer, and POZ domain interaction interfaces represent an attractive target for therapeutic intervention. Miz-1 (Myc-interacting zinc-finger protein) is a POZ-ZF factor that regulates DNA-damage-induced cell cycle arrest and plays an important role in human cancer by virtue of its interaction with the c-Myc and BCL6 oncogene products. The Miz-1 POZ domain mediates both self-association and the recruitment of non-POZ partners. POZ-ZF factors generally function as homodimers, although higher-order associations and heteromeric interactions are known to be physiologically important; crucially, the interaction interfaces in such large complexes have not been characterised. We report here the crystal structure of the Miz-1 POZ domain up to 2.1 A resolution. The tetrameric organisation of Miz-1 POZ reveals two types of interaction interface between subunits; an interface of alpha-helices resembles the dimerisation interface of reported POZ domain structures, whereas a novel beta-sheet interface directs the association of two POZ domain dimers. We show that the beta-sheet interface directs the tetramerisation of the Miz-1 POZ domain in solution and therefore represents a newly described candidate interface for the higher-order homo- and hetero-oligomerisation of POZ-ZF proteins in vivo.

PubMed: 17880999
DOI: 10.1016/j.jmb.2007.08.026

Experimental method

X-RAY DIFFRACTION (2.1 Å)