[Predicting the three-dimensional structure of alpha- and beta-interferons].

O B Ptitsyn; A V Finkel'shteĭn; A G Murzin

PubMed · 3951438

[Predicting the three-dimensional structure of alpha- and beta-interferons].

O B Ptitsyn·A V Finkel'shteĭn·A G Murzin

Abstract

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.

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Animals Circular Dichroism Humans Interferon Type I Models, Molecular Peptide Fragments Protein Conformation Scattering, Radiation English Abstract Journal Article

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O B Ptitsyn, A V Finkel'shteĭn, A G Murzin. [Predicting the three-dimensional structure of alpha- and beta-interferons].. https://pubmed.ncbi.nlm.nih.gov/3951438/

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