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.
journal_name
Genome Resjournal_title
Genome researchauthors
Duret L,Guex N,Peitsch MC,Bairoch Adoi
10.1101/gr.8.4.348subject
Has Abstractpub_date
1998-04-01 00:00:00pages
348-53issue
4eissn
1088-9051issn
1549-5469journal_volume
8pub_type
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