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- W2021495597 abstract "Abstract Human interleukin‐2 (IL‐2) α helix B is more conserved than the whole molecule, but has been less studied than other α helices of IL‐2. Using site‐directed mutagenesis, several IL‐2 mutants in this helix were obtained. We found that the IL‐2 mutant containing Leu at position 62 (Leu 62 ‐IL‐2) loses its ability to bind IL‐2 receptor subunit α (IL‐2Rα), but retains binding affinity to IL‐2R subunit βγ as well as some bioactivity; nevertheless, another substitution at the same residue, Arg 62 IL‐2, loses its binding ability to both IL‐2Rα and IL‐2Rβγ, and can no longer stimulate IL‐2‐dependent cell growth, showing that Glu 62 not only takes part in IL‐2Rα binding, but can also affect IL‐2 binding to IL‐2Rβγ. In this regard, Glu 62 may be a key site in the IL‐2/IL‐2Rα interaction, and can facilitate IL‐2R ternary‐complex formation, leading to IL‐2Rα‐mediated, IL‐2‐stimulated signal transduction." @default.
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- W2021495597 date "1995-05-01" @default.
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- W2021495597 title "Substitutions at the Glu62 residue of human interleukin-2 differentially affect its binding to the α chain and the βγ complex of the interleukin-2 receptor" @default.
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- W2021495597 doi "https://doi.org/10.1002/eji.1830250512" @default.
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