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
Institution
Titre
New insulin-like proteins with atypical disulfide bond pattern characterized in Caenorhabditis elegans by comparative sequence analysis and homology modeling.
Périodique
Genome research
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
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 16:02
Dernière modification de la notice
30/01/2021 7:26