Structure of recombinant bovine interferon-γ at 3.0 Å resolution

Abstract

The three-dimensional crystal structure of recombinant bovine interferon-gamma was determined using the multiple isomorphous replacement method at 3.0 A and refined to an R factor of 19.2%. This protein crystallizes in space group P2(1)2(1)2(1) with unit-cell parameters of a = 42.8, b = 79.9 and c = 85.4 A. There is one functional dimer in the asymmetric unit. The two polypeptide chains are related by a non-crystallographic twofold symmetry axis. The secondary structure is predominantly alpha-helical with extensive interdigitation of the alpha-helical segments of the polypeptide chains that make up the dimer. The secondary structure, tertiary structure and topology of this molecule are identical to the previously reported structures of recombinant rabbit interferon-gamma and recombinant human interferon-gamma. The molecular topology is also similar to that of murine interferon-beta. These structural similarities strongly indicate the presence of a unique topological feature (fold) among gamma-interferons from different species, and also among the different classes of interferons.

Interleukin‐6: Structure‐function relationships

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Hematopoietic cytokines: Similarities and differences in the structures, with implications for receptor binding

“…(Senda et al, 1992), and interferon-y is a tight dimer in which each chain contains six helices. The helices that form the equivalent of the four-helix bundles discussed above come from both chains (Ealick et al, 1991;Samudzi et al, 1991).…”

Structure and function of interleukin-22 and other members of the interleukin-10 family

“…2a). In IFN-c, a short DE loop is the main reason for a similar structural architecture; however, in IFN-c, the angle formed between the two monomers is *60° [131][132][133][134]. In IL-10, the 90°inter-domain angle allows helix C to be exposed, creating a potential interaction site with its receptors [6].…”