Ptitsyn O B, Finkelstein A V, Murzin A G
FEBS Lett. 1985 Jul 8;186(2):143-8. doi: 10.1016/0014-5793(85)80697-9.
Secondary structures of leucocyte alpha 1- and alpha 2-interferons and of fibroblast beta-interferon are calculated using the molecular theory of protein secondary structures. The common secondary structure calculated for alpha- and beta-interferons is used to predict the three-dimensional structures of fragments 1-110 and 111-166 of the chains (which are supposed to be quasi-independent domains). The predicted structure of the active domain I (1-110) is an 'up-and-down' tetrahelical complex (in which the second helix is shorter than the others and can be absent in alpha 1-interferon) similar to the mirror image of myohaemoerythrin. The predicted structure of domain II (111-166) is either a three-stranded beta-sheet screened from one side by two alpha-helices or a three-helical complex (similar to that in the N-domain of papain), the first structure being more consistent with the circular dichroism data of alpha-interferon and its C-end fragment.
利用蛋白质二级结构的分子理论计算白细胞α1-和α2-干扰素以及成纤维细胞β-干扰素的二级结构。为α-和β-干扰素计算出的共同二级结构用于预测链片段1-110和111-166的三维结构（假定这些片段为准独立结构域）。活性结构域I（1-110）的预测结构是一种“上下”四螺旋复合体（其中第二个螺旋比其他螺旋短，在α1-干扰素中可能不存在），类似于肌血球素的镜像。结构域II（111-166）的预测结构要么是由两条α-螺旋从一侧屏蔽的三链β-折叠，要么是三螺旋复合体（类似于木瓜蛋白酶N结构域中的复合体），第一种结构与α-干扰素及其C端片段的圆二色性数据更一致。
