DNA-binding motifs from eukaryotic transcription factors

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Considerable progress has been made during the past year on structure determinations of eukaryotic transcription factors that function as DNA-binding proteins in concert with RNA polymerase II. New structures include two TATA box-binding proteins bound to distinct TATA elements, two b/HLH/Z factors, Max and USF, recognizing CACGTG, and four helix-turn-helix variants, the third repeat of c-Myb, the POU-specific domain of Oct-1, an atypical homeodomain from LFB1/HNF1, and the fork head domain of HNF-3γ complexed with DNA. Other novel structures include the DNA-binding domain of GATA-1 complexed with DNA, the nucleic acid-binding domain of transcription factor IIS and the five zinc-finger GLI-DNA complex.

Original languageEnglish (US)
Pages (from-to)3-11
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume4
Issue number1
DOIs
StatePublished - Jan 1 1994
Externally publishedYes

Fingerprint

Nucleotide Motifs
Transcription Factors
DNA
TATA-Box Binding Protein
RNA Polymerase II
Phentolamine
Zinc Fingers
DNA-Binding Proteins
Nucleic Acids
Head

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

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DNA-binding motifs from eukaryotic transcription factors. / Burley, Stephen.

In: Current Opinion in Structural Biology, Vol. 4, No. 1, 01.01.1994, p. 3-11.

Research output: Contribution to journalArticle

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