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首页> 外文期刊>Cytokine >How unique is interferon-beta within the type I interferon family?
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How unique is interferon-beta within the type I interferon family?

机译：Inteferon家族内的干扰素β有多独特？

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All type I interferons share structural homology and bind to a common heterodimeric receptor consisting of the IFNAR1 and IFNAR2 subunits, which are expressed on most cell types. Although binding to the same receptor pair, they evoke a broad range of activities within the cell affecting the expression of numerous genes and resulting in profound cellular changes. Differential activation results from multiple levels of cellular and molecular events including binding affinity, receptor density, cell type-specific variations, and post-translational modification of signaling molecules downstream. Within the type I interferon family the Asn-Gly-Arg (NGR) sequence motif is unique to interferon-beta and, together with its deamidated variants Asp-Gly-Arg (DGR) and iso-Asp-Gly-Arg (iso-DGR), imparts additional binding specificities that go beyond that of the canonical IFNAR1/IFNAR2. These warrant further investigations and functional studies and may eventually shed new light on differential effects observed for this molecule in oncology and autoimmune diseases.
机译：所有I型干扰素共享结构性同源性，并与IFNAR1和IFNAR2亚基组成的常见的异二聚体受体结合，其在大多数细胞类型上表达。虽然与相同的受体对结合，但它们在细胞内唤起了影响许多基因表达的细胞内的广泛活性，并导致深细胞变化。差异激活来自多水平的细胞和分子事件，包括结合亲和力，受体密度，细胞类型特异性变化以及信号传导分子下游的后翻透修饰。在I型Interferon系列中，ASN-Gly-Arg（NGR）序列基序是干扰素-β的独特，也与其脱胺变体Asp-Gly-Arg（DGR）和ISO-ASP-甘氨酸（ISO-DGR ），赋予超出规范IFNAR1 / IFNAR2的额外结合特异性。这些保证进一步调查和功能研究，并最终可能对肿瘤和自身免疫疾病中该分子观察到的差异效应上的新光。

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