1AN2

RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN

Summary for 1AN2

• Entry DOI: 10.2210/pdb1an2/pdb
• Descriptor: DNA (5'-D(*GP*TP*GP*TP*AP*GP*GP*TP*CP*AP*CP*GP*TP*GP*AP*CP*C P*TP*AP*CP*AP*C)- 3'), PROTEIN (TRANSCRIPTION FACTOR MAX (TF MAX)) (2 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 16974.85

Authors

Ferre-D'Amare, A.R.,Prendergast, G.C.,Ziff, E.B.,Burley, S.K. (deposition date: 1996-09-06, release date: 1997-09-17, Last modification date: 2024-02-07)

Primary citation

Ferre-D'Amare, A.R.,Prendergast, G.C.,Ziff, E.B.,Burley, S.K.
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.
Nature, 363:38-45, 1993

PubMed 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.

PubMed: 8479534
DOI: 10.1038/363038a0

Experimental method

X-RAY DIFFRACTION (2.9 Å)