2nn2
From Proteopedia
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| - | [[Image:2nn2.gif|left|200px]]<br /> | + | [[Image:2nn2.gif|left|200px]]<br /><applet load="2nn2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2nn2" size=" | + | |
caption="2nn2, resolution 2.10Å" /> | caption="2nn2, resolution 2.10Å" /> | ||
'''Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator'''<br /> | '''Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles | + | BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface, and surfaces for interactions with other factors, including nuclear co-repressors and histone deacetylases. The BTB-ZF protein LRF (also known as ZBTB7, FBI-1, OCZF, and Pokemon) is a master regulator of oncogenesis, and represses the transcription of a variety of important genes, including the ARF, c-fos, and c-myc oncogenes and extracellular matrix genes. We determined the crystal structure of the BTB domain from human LRF to 2.1 A and observed the canonical BTB homodimer fold. However, novel features are apparent on the surface of the homodimer, including differences in the lateral groove and charged pocket regions. The residues that line the lateral groove have little similarity with the equivalent residues from the BCL6 BTB domain, and we show that the 17-residue BCL6 Binding Domain (BBD) from the SMRT co-repressor does not bind to the LRF BTB domain. |
==About this Structure== | ==About this Structure== | ||
| - | 2NN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2NN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Prive, G | + | [[Category: Prive, G G.]] |
| - | [[Category: Stogios, P | + | [[Category: Stogios, P J.]] |
[[Category: btb domain]] | [[Category: btb domain]] | ||
[[Category: candidate oncoprotein]] | [[Category: candidate oncoprotein]] | ||
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[[Category: zinc-finger protein]] | [[Category: zinc-finger protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:37 2008'' |
Revision as of 16:08, 21 February 2008
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Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator
Overview
BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface, and surfaces for interactions with other factors, including nuclear co-repressors and histone deacetylases. The BTB-ZF protein LRF (also known as ZBTB7, FBI-1, OCZF, and Pokemon) is a master regulator of oncogenesis, and represses the transcription of a variety of important genes, including the ARF, c-fos, and c-myc oncogenes and extracellular matrix genes. We determined the crystal structure of the BTB domain from human LRF to 2.1 A and observed the canonical BTB homodimer fold. However, novel features are apparent on the surface of the homodimer, including differences in the lateral groove and charged pocket regions. The residues that line the lateral groove have little similarity with the equivalent residues from the BCL6 BTB domain, and we show that the 17-residue BCL6 Binding Domain (BBD) from the SMRT co-repressor does not bind to the LRF BTB domain.
About this Structure
2NN2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator., Stogios PJ, Chen L, Prive GG, Protein Sci. 2007 Feb;16(2):336-42. Epub 2006 Dec 22. PMID:17189472
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