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Article

A protein engineering approach differentiates the functional importance of carbohydrate moieties of interleukin-5 receptor α.

Biochemistry - 6 Sept 2011

Ishino Tetsuya, Economou Nicoleta J, McFadden Karyn, Zaks-Zilberman Meirav, Jost Monika, Baxter Sabine, Contarino Mark R, Harrington Adrian E, Loll Patrick J, Pasut Gianfranco, Lievens Sam, Tavernier Jan, Chaiken Irwin

Abstract excerpt

Human interleukin-5 receptor α (IL5Rα) is a glycoprotein that contains four N-glycosylation sites in the extracellular region. Previously, we found that enzymatic deglycosylation of IL5Rα resulted in complete loss of IL5 binding. To localize the functionally important carbohydrate moieties, we employed site-directed mutagenesis at the N-glycosylation sites (Asn(15), Asn(111), Asn(196), and Asn(224)). Because...

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PMID: 21770429
DOI: 10.1021/bi2009135

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