Crystal structure of human interferon-γ receptor 2 reveals the structural basis for receptor specificity:

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Abstract

Interferon-γ receptor 2 is a cell-surface receptor that is required for interferon-γ signalling and therefore plays a critical immunoregulatory role in innate and adaptive immunity against viral and also bacterial and protozoal infections. A crystal structure of the extracellular part of human interferon-γ receptor 2 (IFNγR2) was solved by molecular replacement at 1.8?Å resolution. Similar to other class 2 receptors, IFNγR2 has two fibronectin type III domains. The characteristic structural features of IFNγR2 are concentrated in its N-terminal domain: an extensive π-cation motif of stacked residues KWRWRH, a NAG-W-NAG sandwich (where NAG stands for N-acetyl-d-glucosamine) and finally a helix formed by residues 78-85, which is unique among class 2 receptors. Mass spectrometry and mutational analyses showed the importance of N-linked glycosylation to the stability of the protein and confirmed the presence of two disulfide bonds. Structure-based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon-γ and receptor 1, the ligands of IFNγR2.The structure of the extracellular portion of interferon-γ receptor 2, a member of the class II cytokine receptors, has been solved. Bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and identified a putative binding site for interferon-γ.

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Mikulecký, P., Zahradník, J., Kolenko, P., Černý, J., Charnavets, T., Kolářová, L., … Schneider, B. (2016). Crystal structure of human interferon-γ receptor 2 reveals the structural basis for receptor specificity: Acta Crystallographica Section D: Structural Biology, 72(9), 1017–1025. https://doi.org/10.1107/S2059798316012237

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