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2q81
From Proteopedia
(New page: 200px<br /> <applet load="2q81" size="450" color="white" frame="true" align="right" spinBox="true" caption="2q81, resolution 2.100Å" /> '''Crystal Structure ...) |
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caption="2q81, resolution 2.100Å" /> | caption="2q81, resolution 2.100Å" /> | ||
'''Crystal Structure of the Miz-1 BTB/POZ domain'''<br /> | '''Crystal Structure of the Miz-1 BTB/POZ domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2Q81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PG4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2Q81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q81 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:22:35 2008'' |
Revision as of 10:22, 23 January 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
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