Structural model for interferons

• Published in: FEBS letters Vol. 186; no. 2; pp. 143 - 148
• Main Authors: Ptitsyn, O.B., Finkelstein, A.V., Murzin, A.G.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 08-07-1985; Elsevier
• Subjects: alpha -interferon; beta -interferon; Biological and medical sciences; Circular Dichroism; fibroblasts; Fundamental and applied biological sciences. Psychology; Humans; Interferon; Interferon Type I; Interferon-gamma; leucocytes; Models, Molecular; Molecular biophysics; Peptide Fragments - analysis; primary structure; Protein Conformation; Protein secondary structure prediction; Protein tertiary structure prediction; Structure in molecular biology; tertiary structure; Tridimensional structure; Protein secondary structure prediction; Interferon; Protein tertiary structure prediction; Proteins; Alpha interferon; Tertiary structure; Β-Structure; Beta interferon; Prediction; Models; Helical structure; Secondary structure; Conformation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(85)80697-9

Secondary structures of leucocyte α
1- and α
2-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 α
1-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.