Resonance assignments, secondary structure and 15N relaxation data of the human transcriptional coactivator hMBF1 (57-148).
Multiprotein bridging factor 1 (MBF1) is a transcriptional coactivator that is thought to bridge between the TATA box-binding protein (TBP) and DNA binding regulatory factors, and is conserved from yeast to human. Human MBF1 (hMBF1) can bind to TBP and to the nuclear receptor Ad4BP, and is suggested to mediate Ad4BP-dependent transcriptional activation. Here we report the resonance assignments and secondary structure of hMBF1 (57-148) that contains both TBP binding and activator binding residues. 15N relaxation data were also obtained. As a result, hMBF1 (57-148) was shown to consist of flexible N-terminal residues and a C-terminal domain. The C-terminal domain contains four helices and a conserved C-terminal region.
Mishima
M
M
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Japan.
Ozaki
J
J
Ikegami
T
T
Kabe
Y
Y
Goto
M
M
Ueda
H
H
Hirose
S
S
Handa
H
H
Shirakawa
M
M
D000595:Amino Acid Sequence; D002148:Calmodulin-Binding Proteins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009584:Nitrogen; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics
D002148:Calmodulin-Binding Proteins; C115911:EDF1 protein, human; D015534:Trans-Activators; D009584:Nitrogen