2NN2

Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator

Summary for 2NN2

• Entry DOI: 10.2210/pdb2nn2/pdb
• Descriptor: Zinc finger and BTB domain-containing protein 7A (2 entities in total)
• Functional Keywords: protein-protein interaction domain, transcription repressor, zinc-finger protein, btb domain, candidate oncoprotein, poz domain, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (By similarity): O95365
• Total number of polymer chains: 2
• Total formula weight: 28334.01

Authors

Stogios, P.J.,Chen, L.,Prive, G.G. (deposition date: 2006-10-23, release date: 2006-11-21, Last modification date: 2023-08-30)

Primary citation

Stogios, P.J.,Chen, L.,Prive, G.G.
Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator.
Protein Sci., 16:336-342, 2007

PubMed Abstract: 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.

PubMed: 17189472
DOI: 10.1110/ps.062660907

Experimental method

X-RAY DIFFRACTION (2.1 Å)