Structural model for interferons

Open Access
Publisher Website
Google Scholar
Abstract
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.