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

Détails

ID Serval
serval:BIB_1B3375E88195
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling.
Périodique
Genome research
Auteur(s)
Duret L., Guex N., Peitsch M.C., Bairoch A.
ISSN
1088-9051 (Print)
ISSN-L
1088-9051
Statut éditorial
Publié
Date de publication
04/1998
Peer-reviewed
Oui
Volume
8
Numéro
4
Pages
348-353
Langue
anglais
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
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.
Mots-clé
Amino Acid Sequence, Animals, Caenorhabditis elegans/chemistry, Caenorhabditis elegans/genetics, Disulfides/chemistry, Genes, Helminth, Helminth Proteins/chemistry, Helminth Proteins/genetics, Humans, Insulin/chemistry, Insulin/genetics, Models, Molecular, Molecular Sequence Data, Multigene Family, Sequence Homology, Amino Acid
Pubmed
Web of science
Open Access
Oui
Création de la notice
29/01/2021 15:02
Dernière modification de la notice
30/01/2021 6:26
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