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  • Toll/interleukin-1 receptor domain dimers as the platform for activation and enhanced inhibition of Toll-like receptor signaling [Elektronski vir]
    Fekonja, Ota ; Benčina, Mojca, 1968- ; Jerala, Roman
    TIR (Toll/IL-1 receptor) domains mediate interactions between TLR (Toll-like) or IL-1 family receptors and signaling adapters. While homotypic TIR domain interactions mediate receptor activation they ... are also usurped by microbial TIR-domain containing proteins for immunosuppression. Here we show the role of a dimerized TIR domain platform for the suppression as well as for the activation of MyD88 signaling pathway. Coiled-coil dimerization domain, present in many bacterial TCPs, potently augments suppression of TLR/IL-1R signaling. The addition of a strong coiled-coil dimerization domain conferred the superior inhibition against the wide spectrum of TLRs and prevented the constitutive activation by a dimeric TIR platform. We propose a molecular model of MyD88-mediated signaling based on the dimerization of TIR domains as the limiting step.
    Source: Journal of biological chemistry [Elektronski vir]. - ISSN 1083-351X (Vol. 287, no. 37, 7 Sep. 2012, str. 30993-31002)
    Type of material - e-article ; adult, serious
    Publish date - 2012
    Language - english
    COBISS.SI-ID - 5026586

    Link(s):

    http://www.jbc.org/content/early/2012/07/24/jbc.M112.376186.full.pdf+html?sid=b51120e9-84e2-4294-85c0-bccab8f1f1b5
    DOI

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