2q81
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The POZ/BTB domain is an evolutionarily conserved motif found in | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | A | + | A beta-sheet interaction interface directs the tetramerisation of the Miz-1 POZ domain., Stead MA, Trinh CH, Garnett JA, Carr SB, Baron AJ, Edwards TA, Wright SC, J Mol Biol. 2007 Nov 2;373(4):820-6. Epub 2007 Aug 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17880999 17880999] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carr, S | + | [[Category: Carr, S B.]] |
| - | [[Category: Edwards, T | + | [[Category: Edwards, T A.]] |
| - | [[Category: Garnett, J | + | [[Category: Garnett, J A.]] |
| - | [[Category: Stead, M | + | [[Category: Stead, M A.]] |
| - | [[Category: Trinh, C | + | [[Category: Trinh, C H.]] |
| - | [[Category: Wright, S | + | [[Category: Wright, S C.]] |
[[Category: PG4]] | [[Category: PG4]] | ||
[[Category: btb/poz domain]] | [[Category: btb/poz domain]] | ||
[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:37:00 2008'' |
Revision as of 16:37, 21 February 2008
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Crystal Structure of the Miz-1 BTB/POZ domain
Overview
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.
About this Structure
2Q81 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
A beta-sheet interaction interface directs the tetramerisation of the Miz-1 POZ domain., Stead MA, Trinh CH, Garnett JA, Carr SB, Baron AJ, Edwards TA, Wright SC, J Mol Biol. 2007 Nov 2;373(4):820-6. Epub 2007 Aug 21. PMID:17880999
Page seeded by OCA on Thu Feb 21 18:37:00 2008
