Resonance assignments, secondary structure and N-15 relaxation data of thehuman 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 bi nding 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 contai ns both TBP binding and activator binding residues. N-15 relaxation data we re also obtained. As a result, hMBF1 (57-148) was shown to consist of flexi ble N-terminal residues and a C-terminal domain. The C-terminal domain cont ains four helices and a conserved C-terminal region.