3DI3

Crystal structure of the complex of human interleukin-7 with glycosylated human interleukin-7 receptor alpha ectodomain

3DI3 の概要

• エントリーDOI: 10.2210/pdb3di3/pdb
• 関連するPDBエントリー: 3DI2
• 分子名称: Interleukin-7, Interleukin-7 receptor subunit alpha, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: interleukin, cytokine, cytokine receptor, ectodomain, glycoprotein, growth factor, secreted, disease mutation, membrane, phosphoprotein, receptor, scid, transmembrane, cytokine-cytokine receptor complex, cytokine/cytokine receptor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44509.68

構造登録者

McElroy, C.A.,Dohm, J.A.,Walsh, S.T.R. (登録日: 2008-06-19, 公開日: 2009-01-27, 最終更新日: 2024-10-16)

主引用文献

McElroy, C.A.,Dohm, J.A.,Walsh, S.T.
Structural and Biophysical Studies of the Human IL-7/IL-7Ralpha Complex.
Structure, 17:54-65, 2009

PubMed Abstract: IL-7 and IL-7Ralpha bind the gamma(c) receptor, forming a complex crucial to several signaling cascades leading to the development and homeostasis of T and B cells. We report that the IL-7Ralpha ectodomain uses glycosylation to modulate its binding constants to IL-7, unlike the other receptors in the gamma(c) family. IL-7 binds glycosylated IL-7Ralpha 300-fold more tightly than unglycosylated IL-7Ralpha, and the enhanced affinity is attributed primarily to an accelerated on rate. Structural comparison of IL-7 in complex to both forms of IL-7Ralpha reveals that glycosylation does not participate directly in the binding interface. The SCID mutations of IL-7Ralpha locate outside the binding interface with IL-7, suggesting that the expressed mutations cause protein folding defects in IL-7Ralpha. The IL-7/IL-7Ralpha structures provide a window into the molecular recognition events of the IL-7 signaling cascade and provide sites to target for designing new therapeutics to treat IL-7-related diseases.

PubMed: 19141282
DOI: 10.1016/j.str.2008.10.019

実験手法

X-RAY DIFFRACTION (2.9 Å)