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Sequence similarity between opioid peptide precursors and dna-binding proteins

Academic Article
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Overview

authors

  • Bakalkin, G. Y.
  • Ponomariev, D.
  • Sarkisyan, R. A.
  • Terenius, Lars

publication date

  • 1991

journal

  • FEBS Letters  Journal

abstract

  • The opioid peptide precursors, preprodynorphin and preproenkephalin show structure similarity with a transcription factor, hunchback and the putative helix-loop-helix DNA-binding proteins, lil-1, tal and twist. Segments with similarity contain the three enkephalin sequences in preprodynorphin and one in preproenkephalin which are present within heptapeptide repeats characteristic of an alpha-helical coiled-coil structure distinctive of an amphipathic helix-loop-helix DNA-binding motif. Hunchback and the opioid prohormones also have cystein-rich regions characteristic of zinc-finger domains in common.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • DNA
  • DNA-Binding Proteins
  • Dynorphins
  • Enkephalins
  • Humans
  • Molecular Sequence Data
  • Protein Precursors
  • Sequence Homology, Nucleic Acid
  • Transcription Factors
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Research

keywords

  • DNA-BINDING PROTEIN
  • OPIOID PRECURSOR
  • SEQUENCE HOMOLOGY
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(91)80471-e

PubMed ID

  • 1673934
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Additional Document Info

start page

  • 175

end page

  • 177

volume

  • 282

issue

  • 1

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