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Published online before print December 22, 2006
Protein Science, DOI: 10.1110/ps.062660907
 Copyright © 2006 The Protein Society
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PROTEIN STRUCTURE REPORT

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

Peter J. Stogios1, Lu Chen2, and Gilbert G. Privé1,2,3

1 Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada
2 Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 1L7, Canada
3 Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada

(RECEIVED November 8, 2006; FINAL REVISION November 8, 2006; ACCEPTED November 13, 2006)

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 Å 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.

Keywords: BTB; POZ; LRF; ZBTB7; SMRT; transcription repression; X-ray crystallography

Reprint requests to: Gilbert G. Privé, Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Departments of Medical Biophysics and Biochemistry, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada; e-mail: prive{at}uhnres.utoronto.ca; fax: (416) 581-7562.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062660907.


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