Assignment of 1H, 15N, 13C, resonances, identification of elements of secondary structure and determination of the global fold of the DNA-binding domain of GAL4

Extensive assignments of the 1H, 15N and 13C resonances of the N-terminal DNA-binding domain of the GAL4 transactivator protein were obtained from two- and three-dimensional heteronuclear NMR experiments and structural studies based on short-, medium- and long-range NOEs, which establish the global fold of the protein. The results indicate that the peptide consists of two short alpha helices. The obtained solution structure is similar to previously determined structures of GAL4.