Summary information and primary citation
- PDB-id
-
1an2;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.9 Å)
- Summary
- Recognition by max of its cognate DNA through a dimeric
b-hlh-z domain
- Reference
-
Ferre-D'Amare AR, Prendergast GC, Ziff EB, Burley SK
(1993): "Recognition
by Max of its cognate DNA through a dimeric b/HLH/Z
domain." Nature, 363,
38-45. doi: 10.1038/363038a0.
- Abstract
- 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 A resolution.
Max binds as a dimer to its recognition sequence CACGTG by
direct contacts between the alpha-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 alpha-helical segments
separated by a loop. The two alpha-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.
