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

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 Res

journal_title

Genome research

authors

Duret L,Guex N,Peitsch MC,Bairoch A

doi

10.1101/gr.8.4.348

subject

Has Abstract

pub_date

1998-04-01 00:00:00

pages

348-53

issue

4

eissn

1088-9051

issn

1549-5469

journal_volume

8

pub_type

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