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Structural model for interferons
Author(s) -
Ptitsyn O.B.,
Finkelstein A.V.,
Murzin A.G.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80697-9
Subject(s) - protein secondary structure , circular dichroism , alpha interferon , papain , alpha helix , helix (gastropod) , alpha (finance) , protein structure , protein tertiary structure , chemistry , beta (programming language) , interferon , stereochemistry , crystallography , biology , virology , mathematics , biochemistry , enzyme , ecology , construct validity , statistics , snail , computer science , programming language , psychometrics
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.