Abstract
Interleukin-36α (IL-36α) is a recently characterised member of the interleukin-1 superfamily. It is involved in the pathogenesis of inflammatory arthritis in one third of psoriasis patients. By binding of IL-36α to its receptor IL-36R via the NF-κB pathway other cytokines involved in inflammatory and apoptotic cascade are activated. The efficacy of complex formation is controlled by N-terminal processing. To obtain a more detailed view on the structure function relationship we performed a heteronuclear multidimensional NMR investigation and here report the 1H, 13C, and 15N resonance assignments for the backbone and side chain nuclei of the pro-inflammatory cytokine interleukin-36α.
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Acknowledgments
Financial support by the Deutsche Forschungsgemeinschaft (DFG) within FOR 1738 (to D.I. and O.O.) is gratefully acknowledged. This work was partially supported by the BMBF network ProNet-T3 “Protein competence center Halle: tools, targets & therapeutics”. The FLI is a member of the Leibniz Association (WGL) and is financially supported by the Federal Government of Germany and the State of Thuringia.
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Dedicated to Heinrich Rüterjans on the occasion of his 80th birthday.
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Goradia, N., Wißbrock, A., Wiedemann, C. et al. 1H, 13C, and 15N resonance assignments for the pro-inflammatory cytokine interleukin-36α. Biomol NMR Assign 10, 329–333 (2016). https://doi.org/10.1007/s12104-016-9694-7
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DOI: https://doi.org/10.1007/s12104-016-9694-7