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  • Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains

    Author(s)
    Ve, Thomas
    Williams, Simon J
    Kobe, Bostjan
    Griffith University Author(s)
    Ve, Thomas
    Year published
    2015
    Metadata
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    Abstract
    The Toll/interleukin-1 receptor/resistance protein (TIR) domain is a protein–protein interaction domain consisting of 125–200 residues, widely distributed in animals, plants and bacteria but absent from fungi, archea and viruses. In plants and animals, these domains are found in proteins with functions in innate immune pathways, while in bacteria, some TIR domain-containing proteins interfere with the innate immune pathways in the host. TIR domains function as protein scaffolds, mostly involving self-association and homotypic interactions with other TIR domains. In the last 15 years, the three-dimensional structures of TIR ...
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    The Toll/interleukin-1 receptor/resistance protein (TIR) domain is a protein–protein interaction domain consisting of 125–200 residues, widely distributed in animals, plants and bacteria but absent from fungi, archea and viruses. In plants and animals, these domains are found in proteins with functions in innate immune pathways, while in bacteria, some TIR domain-containing proteins interfere with the innate immune pathways in the host. TIR domains function as protein scaffolds, mostly involving self-association and homotypic interactions with other TIR domains. In the last 15 years, the three-dimensional structures of TIR domains from several mammalian, plant and bacterial proteins have been reported. These structures, jointly with functional data including the identification of interacting proteins, have started to provide insight into the molecular basis of the assembly of animal and plant immune signaling complexes, and for host immunosuppression by bacterial pathogens. This review focuses on the current knowledge of the structures of the TIR domains and how the structure relates to function.
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    Journal Title
    Apoptosis
    Volume
    20
    DOI
    https://doi.org/10.1007/s10495-014-1064-2
    Subject
    Biochemistry and cell biology
    Biochemistry and cell biology not elsewhere classified
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/172916
    Collection
    • Journal articles

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