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English

New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling

Contributors

Duret, Laurent; Guex, Nicolas; Peitsch, Manuel C; Bairoch, Amos Marc

Published in

Genome research, vol. 8, no. 4, p. 348-353

Publication date

1998

Abstract

We have identified three new families of insulin homologs in Caenorhabditis elegans. In two of these families, concerted mutations suggest that an additional disulfide bond links B and A domains, and that the A-domain internal disulfide bond is substituted by a hydrophobic interaction. Homology modeling remarkably confirms these predictions and shows that despite this atypical disulfide bond pattern and the absence of C-like peptide, all these proteins may adopt the same fold as the insulin. Interestingly, whereas we identified 10 insulin-like peptides, only one insulin-like-receptor (daf-2) has been found. We propose that these insulin-related peptides may correspond to different activators or inhibitors of the daf-2 insulin-regulating pathway.

Keywords

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans/chemistry/genetics
  • Disulfides/chemistry
  • Genes, Helminth
  • Helminth Proteins/chemistry/genetics
  • Humans
  • Insulin/chemistry/genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family
  • Sequence Homology, Amino Acid

UNIGE affiliation entities

UNIGE research groups

Citation (ISO format)

DURET, Laurent et al. New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling. In: Genome research, 1998, vol. 8, n° 4, p. 348–353. doi: 10.1101/gr.8.4.348

Main files (1)

Article (Published version)

Identifiers

Journal ISSN

1088-9051
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180downloads

Technical informations

Creation

22/07/2015 08:59:00

First validation

22/07/2015 08:59:00

Update

30/03/2023 10:34:31

Status update

30/03/2023 10:34:31

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