TY - JOUR
T1 - Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
AU - Ferré-D'Amaré, Adrian R.
AU - Prendergast, George C.
AU - Ziff, Edward B.
AU - Burley, Stephen K.
PY - 1993
Y1 - 1993
N2 - The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 Å resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the α-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two α-helical segments separated by a loop. The two α-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
AB - The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 Å resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the α-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two α-helical segments separated by a loop. The two α-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
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U2 - 10.1038/363038a0
DO - 10.1038/363038a0
M3 - Article
C2 - 8479534
AN - SCOPUS:0027910469
SN - 0028-0836
VL - 363
SP - 38
EP - 45
JO - Nature
JF - Nature
IS - 6424
ER -