Crystals of ternary protein-DNA complexes composed of DNA-binding domains of c-Myb or v-Myb, C/EBPα or C/EBPβ and tom-1A promoter fragment

T. H. Tahirov, M. Sasaki, T. Inoue-Bungo, A. Fujikawa, K. Sato, T. Kumasaka, M. Yamamoto, K. Ogata

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

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/EBPα or C/EBPβ 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.

Original languageEnglish (US)
Pages (from-to)1655-1658
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number11
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • Structural Biology

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