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2q81

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[[Image:2q81.jpg|left|200px]]
[[Image:2q81.jpg|left|200px]]
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{{Structure
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|GENE= ZBTB17, MIZ1, ZNF151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2q81| PDB=2q81 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q81 OCA], [http://www.ebi.ac.uk/pdbsum/2q81 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q81 RCSB]</span>
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'''Crystal Structure of the Miz-1 BTB/POZ domain'''
'''Crystal Structure of the Miz-1 BTB/POZ domain'''
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[[Category: Trinh, C H.]]
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[[Category: Wright, S C.]]
[[Category: Wright, S C.]]
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[[Category: btb/poz domain]]
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[[Category: Btb/poz domain]]
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[[Category: transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:30:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:46:01 2008''
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Revision as of 11:30, 4 May 2008

Template:STRUCTURE 2q81

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. 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 Sun May 4 14:30:21 2008

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