2q81: Difference between revisions

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==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.

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==

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==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17880999 17880999]

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: Single protein]]

[[Category: Carr, S.B.]]

[[Category: Carr, S B.]]

[[Category: Edwards, T.A.]]

[[Category: Edwards, T A.]]

[[Category: Garnett, J.A.]]

[[Category: Garnett, J A.]]

[[Category: Stead, M.A.]]

[[Category: Stead, M A.]]

[[Category: Trinh, C.H.]]

[[Category: Trinh, C H.]]

[[Category: Wright, S.C.]]

[[Category: Wright, S C.]]

[[Category: PG4]]

[[Category: btb/poz domain]]

[[Category: transcription]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 10: / Line 10: @@
 ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17880999 17880999]
+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: Single protein]]
-[[Category: Carr, S.B.]]
+[[Category: Carr, S B.]]
-[[Category: Edwards, T.A.]]
+[[Category: Edwards, T A.]]
-[[Category: Garnett, J.A.]]
+[[Category: Garnett, J A.]]
-[[Category: Stead, M.A.]]
+[[Category: Stead, M A.]]
-[[Category: Trinh, C.H.]]
+[[Category: Trinh, C H.]]
-[[Category: Wright, S.C.]]
+[[Category: Wright, S C.]]
 [[Category: PG4]]
 [[Category: btb/poz domain]]
 [[Category: transcription]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:22:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:37:00 2008''