2q81
From Proteopedia
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|PDB= 2q81 |SIZE=350|CAPTION= <scene name='initialview01'>2q81</scene>, resolution 2.100Å | |PDB= 2q81 |SIZE=350|CAPTION= <scene name='initialview01'>2q81</scene>, resolution 2.100Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | + | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ZBTB17, MIZ1, ZNF151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ZBTB17, MIZ1, ZNF151 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Trinh, C H.]] | [[Category: Trinh, C H.]] | ||
[[Category: Wright, S C.]] | [[Category: Wright, S C.]] | ||
| - | [[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 Mon Mar 31 04:46:01 2008'' |
Revision as of 01:46, 31 March 2008
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| , resolution 2.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ZBTB17, MIZ1, ZNF151 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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