[Predicting the three-dimensional structure of alpha- and beta-interferons].
Secondary structures of leukocyte 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 missed 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 better consistent with the circular dichroism data of alpha-interferon and its C-end fragment.
D000818:Animals; D002942:Circular Dichroism; D006801:Humans; D007370:Interferon Type I; D008958:Models, Molecular; D010446:Peptide Fragments; D011487:Protein Conformation; D012542:Scattering, Radiation
D007370:Interferon Type I; D010446:Peptide Fragments
Predskazanie prostranstvennoĭ struktury alpha- i beta-interferonov.