Structural model for interferons

FEBS Letters

Ptitsyn, O.B.¹  Murzin, A.G.¹  Finkelstein, A.V.¹ 

[1] Institute of Protein Research. Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: Interferon;    Protein secondary structure prediction;    Protein tertiary structure prediction;   

DOI  :  10.1016/0014-5793(85)80697-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Secondary structures of leucocyte α₁- and α₂-interferons and of fibroblast β-interferon are calculated using the molecular theory of protein secondary structures. The common secondary structure calculated for α- and β-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 α₁-interferon) similar to the mirror image of myohaemoerythrin. The predicted structure of domain II (111–166) is either a three-stranded β-sheet screened from one side by two α-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 α-interferon and its C-end fragment.

【 授权许可】

Unknown