7E0E

Crystal structure of mouse interferon alpha2 at 2.1 angstrom resolution

Summary for 7E0E

• Entry DOI: 10.2210/pdb7e0e/pdb
• Descriptor: Interferon alpha-2, GLYCEROL, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: interferon, immune system, mouse, cytokine
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 19850.63

Authors

Watanabe, H.,Yabe-Wada, T.,Unno, M. (deposition date: 2021-01-27, release date: 2021-04-07, Last modification date: 2024-11-13)

Primary citation

Watanabe, H.,Yabe-Wada, T.,Onai, N.,Unno, M.
Detailed structure of mouse interferon alpha 2 and its interaction with Sortilin.
J.Biochem., 170:265-273, 2021

PubMed Abstract: Interferon α (IFNα) is a type I interferon, an essential cytokine employed by the immune system to fight viruses. Although a number of the structures of type I interferons have been reported, most of the known structures of IFNα are in complex with its receptors. There are only two examples of structures of free IFNα: one is a dimeric X-ray structure without side-chain information; and another is an NMR structure of human IFNα. Although we have shown that Sortilin is involved in the secretion of IFNα, the details of the molecular interaction and the secretion mechanism remain unclear. Recently, we solved the X-ray structure of mouse Sortilin, but the structure of mouse IFNα remained unknown. In this study, we determined the crystal structure of mouse IFNα2 at 2.1 Å resolution and investigated its interaction with Sortilin. Docking simulations suggested that Arg22 of mouse IFNα2 is important for the interaction with mouse Sortilin. Mutation of Arg22 to alanine facilitated IFNα2 secretion, as determined by flow cytometry, highlighting the contribution of this residue to the interaction with Sortilin. These results suggest an important role for Arg22 in mouse IFNα for Sortilin-mediated IFNα trafficking.

PubMed: 33769476
DOI: 10.1093/jb/mvab038

Experimental method

X-RAY DIFFRACTION (2.102 Å)