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Search query: Toll/interleukin-1 receptor
15 articles match your search "Toll/interleukin-1 receptor"Results 1 to 10, sorted by relevance:
![m logo](https://journals.iucr.org/logos/jicons/m_36x36.png)
The TIR (Toll/interleukin-1 receptor) domains are found in proteins with roles in the immune systems of humans, plants and bacteria. A combination of structural methods ranging from X-ray and electron crystallography to cryogenic electron microscopy and nuclear magnetic resonance spectroscopy has been required to understand how these domains contribute to signalling, highlighting the complementarity of different structural approaches.
![f logo](https://journals.iucr.org/logos/jicons/f_36x36.png)
IL-18 and its two receptors, IL-18Rα and IL-18Rβ, were purified for crystallization and biochemical analysis. IL-18 was crystallized in free, IL-18Rα-bound and IL-18Rα/IL-18Rβ-bound states and complete X-ray data sets suitable for further structural analysis were obtained from each crystal.
![d logo](https://journals.iucr.org/logos/jicons/d_36x36.png)
The innate immune receptor TLR8 can be positively or negatively regulated by small chemical ligands. Structural views of agonist-bound and antagonist-bound forms have revealed the mechanisms underlying agonism and antagonism.
![f logo](https://journals.iucr.org/logos/jicons/f_36x36.png)
This report describes the crystallization and preliminary structure determination of the TIR domain from a plant disease-resistance protein.
![d logo](https://journals.iucr.org/logos/jicons/d_36x36.png)
The structural and functional characterization of the N-terminal domain of the Toll-like receptor signalling adaptor TRIF/TICAM-1 is presented. The 2.22 Å resolution crystal structure was determined by selenomethionine-based SAD phasing using a protein containing two additional introduced methionines.
![f logo](https://journals.iucr.org/logos/jicons/f_36x36.png)
Crystallization of the cystine-knot protein Spätzle occurred following serendipitous limited degradation of the pro-Spätzle propeptide during the crystallization experiment.
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Signal transduction in the Toll-like receptor and interleukin-1 receptor pathways requires both kinase activation and ubiquitination. Here, we will present our recent structural studies on critical mediators of the pathways.
![f logo](https://journals.iucr.org/logos/jicons/f_36x36.png)
Phylogenetic and structural characterization of the only predicted leucine-rich repeat-containing protein from the human pathogen Treponema pallidum is reported.
![d logo](https://journals.iucr.org/logos/jicons/d_36x36.png)
Crystal structure of the SEFIR domain from human IL-17 receptor A provides new insights into IL-17 signaling.
![f logo](https://journals.iucr.org/logos/jicons/f_36x36.png)
To investigate the molecular basis of immune signalling initiated by the TIR domains of plant disease-resistance proteins, the crystallization and preliminary X-ray diffraction analyses of the TIR domains of three proteins involved in disease resistance in A. thaliana are reported.