Structure-function relationship in a β-sheet peptide Inhibitor of E47 dimerization and DNA binding

Indraneel Ghosh, Roy Issac, Jean Chmielewski

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

A β-sheet peptide inhibitor, 2H10, has been developed that inhibits the dimerization of the transcription factor E47. Inhibition of E47 dimerization has been demonstrated to also inhibit the DNA binding of this transcription factor. Truncated peptides based on 2H10 have demonstrated that the β-sheet content of these peptides directly correlates with their inhibitory properties. Individual residues within 2H10 were identified that were responsible for the β-sheet secondary structure by employing an alanine replacement strategy. The β-sheet character of the alanine mutants also correlated well with their inhibition of E47 DNA binding. These results provide further evidence that interactions between the interfacial peptide inhibitors of E47 and the transcription factor itself are mediated by a β-sheet structure. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)61-66
Number of pages6
JournalBioorganic and Medicinal Chemistry
Volume7
Issue number1
DOIs
StatePublished - Jan 1999
Externally publishedYes

Fingerprint

Dimerization
Transcription Factors
Alanine
Peptides
DNA

Keywords

  • Dimer
  • Inhibitor
  • Peptide
  • Transcription factor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Structure-function relationship in a β-sheet peptide Inhibitor of E47 dimerization and DNA binding. / Ghosh, Indraneel; Issac, Roy; Chmielewski, Jean.

In: Bioorganic and Medicinal Chemistry, Vol. 7, No. 1, 01.1999, p. 61-66.

Research output: Contribution to journalArticle

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