7E0E

Crystal structure of mouse interferon alpha2 at 2.1 angstrom resolution

7E0E の概要

• エントリーDOI: 10.2210/pdb7e0e/pdb
• 分子名称: Interferon alpha-2, GLYCEROL, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: interferon, immune system, mouse, cytokine
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19850.63

構造登録者

Watanabe, H.,Yabe-Wada, T.,Unno, M. (登録日: 2021-01-27, 公開日: 2021-04-07, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.102 Å)