Crystals of ternary protein-DNA complexes composed of DNA-binding domains of c-Myb or v-Myb, C/EBPalpha or C/EBPbeta and tom-1A promoter fragment
| Autor: | Takashi Kumasaka, Kazuhiro Ogata, Ko Sato, Taiko Inoue-Bungo, Motoko Sasaki, Tahir H. Tahirov, Masaki Yamamoto, Atsushi Fujikawa |
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| Rok vydání: | 2001 |
| Předmět: |
animal structures
Protein Conformation Biology Crystallography X-Ray Oncogene Proteins v-myb Proto-Oncogene Proteins c-myb Protein structure Structural Biology CCAAT-Enhancer-Binding Protein-alpha Animals Humans A-DNA MYB Bacteriophages Promoter Regions Genetic Gene Point mutation CCAAT-Enhancer-Binding Protein-beta fungi Intracellular Signaling Peptides and Proteins Proteins General Medicine DNA-binding domain Molecular biology Rats Nucleic Acid Conformation Crystallization |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 57(Pt 11) |
| ISSN: | 0907-4449 |
| Popis: | c-Myb and the C/EBP family are transcriptional regulatory factors that act in concert to regulate the expression of myeloid-specific genes. v-Myb encoded by avian myeloblastosis virus (AMV) is a mutated form of c-Myb that contains point mutations which disrupt the cooperation with C/EBPs. To understand the mechanism of the transcriptional synergy between c-Myb and C/EBPs and the effect of the v-Myb mutations on that synergy, knowledge based on their three-dimensional structures is essential. Crystals of ternary complexes, in which various combinations of the DNA-binding domains of c-Myb or v-Myb and C/EBPalpha or C/EBPbeta are bound to a DNA fragment from tom-1A promoter, were obtained by the vapour-diffusion method. Complete diffraction data sets were obtained from each native crystal and two types of iodine-derivative crystals. A three-wavelength MAD data set was also obtained from a bromine-derivative crystal. |
| Databáze: | OpenAIRE |
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