TY - JOUR
AU - Clore, G. Marius
AB - The structure of a complex between the DMA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2–His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger–DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD–DNA complex for chromatin remodelling are discussed.
TI - The solution structure of a specific GAGA factor–DNA complex reveals a modular binding mode
JF - Nature Structural & Molecular Biology
DO - 10.1038/nsb0297-122
DA - 1997-02-01
UR - https://www.deepdyve.com/lp/springer-journals/the-solution-structure-of-a-specific-gaga-factor-dna-complex-reveals-a-ZtamQOCI0a
SP - 122
EP - 132
VL - 4
IS - 2
DP - DeepDyve
ER -