Crystal structure of the BTB domain from PLZF
Autor: | K.F. Ahmad, Gilbert G. Privé, Christian K Engel |
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Rok vydání: | 1998 |
Předmět: |
Protein Conformation
Molecular Sequence Data Kruppel-Like Transcription Factors Biology Ligands DNA-binding protein Kelch motif Protein structure X-Ray Diffraction Humans Promyelocytic Leukemia Zinc Finger Protein Amino Acid Sequence Nuclear protein BTB/POZ domain Transcription factor Zinc finger Binding Sites Multidisciplinary Sequence Homology Amino Acid Zinc Fingers Biological Sciences Molecular biology Cell biology DNA-Binding Proteins Histone deacetylase complex Transcription Factors |
Zdroj: | Proceedings of the National Academy of Sciences. 95:12123-12128 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.95.21.12123 |
Popis: | The BTB domain (also known as the POZ domain) is an evolutionarily conserved protein–protein interaction motif found at the N terminus of 5–10% of C 2 H 2 -type zinc-finger transcription factors, as well as in some actin-associated proteins bearing the kelch motif. Many BTB proteins are transcriptional regulators that mediate gene expression through the control of chromatin conformation. In the human promyelocytic leukemia zinc finger (PLZF) protein, the BTB domain has transcriptional repression activity, directs the protein to a nuclear punctate pattern, and interacts with components of the histone deacetylase complex. The association of the PLZF BTB domain with the histone deacetylase complex provides a mechanism of linking the transcription factor with enzymatic activities that regulate chromatin conformation. The crystal structure of the BTB domain of PLZF was determined at 1.9 Å resolution and reveals a tightly intertwined dimer with an extensive hydrophobic interface. Approximately one-quarter of the monomer surface area is involved in the dimer intermolecular contact. These features are typical of obligate homodimers, and we expect the full-length PLZF protein to exist as a branched transcription factor with two C-terminal DNA-binding regions. A surface-exposed groove lined with conserved amino acids is formed at the dimer interface, suggestive of a peptide-binding site. This groove may represent the site of interaction of the PLZF BTB domain with nuclear corepressors or other nuclear proteins. |
Databáze: | OpenAIRE |
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