2nn2
From Proteopedia
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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
Page seeded by OCA on Thu Nov 8 14:53:08 2007
