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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
-
Basic-Leucine Zipper Transcription Factors
-
Cloning, Molecular
-
Computer Simulation
-
DNA / chemistry*
-
DNA / metabolism
-
DNA-Binding Proteins / chemistry*
-
DNA-Binding Proteins / metabolism
-
Escherichia coli
-
Leucine Zippers
-
Macromolecular Substances
-
Mice
-
Models, Molecular
-
Molecular Sequence Data
-
Nucleic Acid Conformation
-
Protein Binding
-
Proto-Oncogene Proteins c-myc / metabolism
-
Transcription Factors / chemistry*
-
Transcription Factors / metabolism
-
X-Ray Diffraction
Substances
-
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
-
Basic-Leucine Zipper Transcription Factors
-
DNA-Binding Proteins
-
Macromolecular Substances
-
Myc associated factor X
-
Proto-Oncogene Proteins c-myc
-
Transcription Factors
-
Max protein, mouse
-
DNA