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首页> 外文期刊>Biochemistry >High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity.
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High-resolution structure of murine interleukin 1 homologue IL-1F5 reveals unique loop conformations for receptor binding specificity.

机译：小鼠白介素1同源物IL-1F5的高分辨率结构揭示了受体结合特异性的独特环构象。

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摘要

Interleukin-1 (IL-1) F5 is a novel member of the IL-1 family. The IL-1 family are involved in innate immune responses to infection and injury. These cytokines bind to specific receptors and cause activation of NFkappaB and MAP kinase. IL-1F5 has a sequence identity of 44% to IL-1 receptor antagonist (IL-1Ra), a natural antagonist of the IL-1 system. Here we report the crystal structure of IL-1F5 to a resolution of 1.6 A. It has the same beta-trefoil fold as other IL-1 family members, and the hydrophobic core is well conserved. However, there are substantial differences in the loop conformations, structures that confer binding specificity for the cognate receptor to IL-1beta and the antagonist IL-1Ra. Docking and superimposition of the IL-1F5 structure suggest that is unlikely to bind to the interleukin1 receptor, consistent with biochemical studies. The structure IL-1F5 lacks features that confer antagonist properties on IL-1Ra, and we predict that like IL-1beta it will act as an agonist. These studiesgive insights into how distinct receptor specificities can evolve within related cytokine families.
机译：白介素-1（IL-1）F5是IL-1家族的新成员。 IL-1家族参与对感染和损伤的先天免疫反应。这些细胞因子与特定受体结合并引起NFkappaB和MAP激酶的激活。 IL-1F5与IL-1系统的天然拮抗剂IL-1受体拮抗剂（IL-1Ra）具有44％的序列同一性。在这里，我们报告了IL-1F5的晶体结构，分辨率为1.6A。它具有与其他IL-1家族成员相同的β-三叶折叠，并且疏水核非常保守。然而，在环构象，赋予同源受体对IL-1β和拮抗剂IL-1Ra的结合特异性的结构上存在实质性差异。与生化研究一致，IL-1F5结构的对接和重叠表明它不太可能与白介素1受体结合。 IL-1F5结构缺乏赋予IL-1Ra拮抗剂特性的功能，并且我们预测与IL-1beta一样它将充当激动剂。这些研究为相关细胞因子家族中不同受体特异性的进化提供了见识。

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