M. Mishima et al., Resonance assignments, secondary structure and N-15 relaxation data of thehuman transcriptional coactivator hMBF1 (57-148), J BIOM NMR, 14(4), 1999, pp. 373-376
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.