Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information

    117028_9150_A Comparative Structural Bioinformatics Analysis of the Insulin Receptor.pdf (815.9Kb)
    Access Status
    Open access
    Authors
    Renteria, Miguel
    Gandhi, Neha
    Vinuesa, P.
    Helmerhorst, Erik
    Mancera, Ricardo
    Date
    2008
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Renteria, Miguel and Gandhi, Neha and Vinuesa, Pablo and Helmerhorst, Erik and Mancera, Ricardo. 2008. A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information. PLoS ONE. 3 (11): pp. 1-15.
    Source Title
    PLoS ONE
    DOI
    10.1371/journal.pone.0003667
    ISSN
    19326203
    Faculty
    Faculty of Health Sciences
    School of Biomedical Sciences
    Remarks

    The link to the journal’s home page is: http://www.plosone.org/home.action

    Copyright: © 2008 Rentería et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

    URI
    http://hdl.handle.net/20.500.11937/29028
    Collection
    • Curtin Research Publications
    Abstract

    The insulin receptor (IR), the insulin-like growth factor 1 receptor (IGF1R) and the insulin receptor-related receptor (IRR) are covalently-linked homodimers made up of several structural domains. The molecular mechanism of ligand binding to the ectodomain of these receptors and the resulting activation of their tyrosine kinase domain is still not well understood. We have carried out an amino acid residue conservation analysis in order to reconstruct the phylogeny of the IR Family. We have confirmed the location of ligand binding site 1 of the IGF1R and IR. Importantly, we have also predicted the likely location of the insulin binding site 2 on the surface of the fibronectin type III domains of the IR. An evolutionary conserved surface on the second leucine-rich domain that may interact with the ligand could not be detected. We suggest a possible mechanical trigger of the activation of the IR that involves a slight 'twist' rotation of the last two fibronectin type III domains in order to face the likely location of insulin. Finally, a strong selective pressure was found amongst the IRR orthologous sequences, suggesting that this orphan receptor has a yet unknown physiological role which may be conserved from amphibians to mammals.

    Related items

    Showing items related by title, author, creator and subject.

    • Structure and function of the insulin receptor: its role during lactation and foetal development
      Deleo, Domenica (1994)
      Prior to the commencement of this study in 1990, a number of reports had appeared in the literature describing the importance of insulin action during lactation in mammals (see Chapter 1). These studies investigated the ...
    • Alzheimer's beta-amyloid peptides compete for insulin binding to the insulin receptor
      Xie, Ling; Helmerhorst, Erik; Plewright, Brian; Van Bronswijk, Wilhelm; Martins, R. (2002)
      The amyloid- (A) peptide is neurotoxic and associated with the pathology of Alzheimer's disease (AD). We investigated the effect of A peptides on insulin binding to the insulin receptor because it is known that (1) A and ...
    • PEDF attenuates insulin-dependent molecular pathways of glucose homeostasis in skeletal myocytes
      Carnagarin, R.; Dharmarajan, Arunasalam; Dass, Crispin (2015)
      Pigment epithelium-derived factor (PEDF) is an anti-angiogenic serpin associated with insulin resistance in metabolic disorders such as diabetes, metabolic syndrome, obesity and polycystic ovarian syndrome. While the ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.