Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer

Tom Ellenberger, Deborah Fass, Martha Arnaud, Stephen C. Harrison

Research output: Contribution to journalArticlepeer-review

346 Scopus citations

Abstract

A large group of transcription factors regulating cell growth and differentiation share a dimeric α-helical DNA-binding domain termed the basic region helix-loop-helix (bHLH). bHLH proteins associate as homodimers and heterodimers having distinctive DNA-binding activities and transcriptional activities that are central to the regulated differentiation of a number of tissues. Some of the bHLH residues specifying these activities have been identified, but a full understanding of their function has awaited further structural information. We report here the crystal structure of the transcription factor E47 bHLH domain bound to DNA. The bHLH of E47 is a parallel, four-helix bundle with structural features that distinguish it from the bHLH-zipper protein Max. The E47 dimer makes nonequivalent contacts to each half of the -CACCTG-binding site. Sequence discrimination at the center of the E box may result from interaction with both the DNA bases and the phosphodiester backbone.

Original languageEnglish
Pages (from-to)970-980
Number of pages11
JournalGenes and Development
Volume8
Issue number8
DOIs
StatePublished - Apr 15 1994

Keywords

  • E box
  • E-protein
  • E47
  • bHLH

Fingerprint

Dive into the research topics of 'Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer'. Together they form a unique fingerprint.

Cite this