Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain

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-helica...

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Veröffentlicht in:	Nature (London) 1993-05, Vol.363 (6424), p.38-45
Hauptverfasser:	Ferré-D'Amaré, Adrian R, Prendergast, George C, Ziff, Edward B, Burley, Stephen K
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Base Sequence Basic Helix-Loop-Helix Leucine Zipper Transcription Factors Basic-Leucine Zipper Transcription Factors Biological and medical sciences Cellular biology Cloning, Molecular Computer Simulation Crystallography Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Escherichia coli Fundamental and applied biological sciences. Psychology Leucine Zippers Macromolecular Substances Mice Models, Molecular Molecular biophysics Molecular Sequence Data Nucleic Acid Conformation Protein Binding Proteins Proto-Oncogene Proteins c-myc - metabolism Structure in molecular biology Transcription Factors - chemistry Transcription Factors - metabolism Tridimensional structure X-Ray Diffraction
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