人类α干扰素介导锌二聚体2 b显示了x射线晶体学。
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Radhakrishnan R,沃尔特LJ, Hruza Reichert P, Trotta PP、Nagabhushan TL,沃尔特先生
人类α干扰素介导锌二聚体2 b显示了x射线晶体学。
结构。1996年12月15日,4 (12):1453 - 63。
- PubMed ID
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8994971 (在PubMed]
- 文摘
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背景:人类α干扰素(huIFN-alpha)家庭显示广谱抗病毒,抗增殖和免疫调节活动多种细胞类型。IFN-alpha是传达的各种生物活性与细胞表面受体的细胞通过特定的相互作用。尽管相当大的努力,但是没有晶体结构尚未报道的这个家庭的一员,因为蛋白质晶体的质量已经不适合晶体研究。直到现在,IFN-alpha的结构性模型都是基于结构的小鼠IFN-beta (muIFN-beta)。这些模型可能不准确,muIFN-beta显著不同的氨基酸序列IFN-alpha提议在受体结合的网站。结构信息huIFN-alpha亚型建模提供一种改进的依据整个IFN-alpha家族的结构。结果:晶体结构重组人类α干扰素的2 b (huIFN-alpha 2 b) 2.9决议决定。HuIFN-alpha 2 b存在于晶体共价的二聚体,同事以小说的方式。与其他结构特征因子,广泛的二聚体交互界面是由锌离子(Zn2 +)。的整体折叠huIFN-alpha 2 b是最类似于muIFN-beta的结构。 Unique to huIFN-alpha 2b is a 3(10) helix in the AB loop which is held to the core of the molecule by a disulfide bond. CONCLUSIONS: The structure of huIFN-alpha 2b provides an accurate model for analysis of the > 15 related type 1 interferon molecules. HuIFN-alpha 2b displays considerable structural similarity with muIFN-beta, interleukin-10 and interferon-gamma, which also bind related class 2 cytokine receptors. From these structural comparisons and numerous studies on the effects of mutations on biological activity, we have identified protein surfaces that appear to be important in receptor activation. This study also reveals the potential biological importance of the huIFN-alpha 2b dimer.