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Title

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

Authors
Guex, Nicolas
Peitsch, Manuel C
Published in Genome Research. 1998, vol. 8, no. 4, p. 348-53
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 SequenceAnimalsCaenorhabditis elegans/chemistry/geneticsDisulfides/chemistryGenes, HelminthHelminth Proteins/chemistry/geneticsHumansInsulin/chemistry/geneticsModels, MolecularMolecular Sequence DataMultigene FamilySequence Homology, Amino Acid
Identifiers
PMID: 9548970
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Research groups Calipho (80)
Institut Suisse de Bioinformatique
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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. 348-53. https://archive-ouverte.unige.ch/unige:74665

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