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4QQV

Extracellular domains of mouse IL-3 beta receptor

4QQV の概要
エントリーDOI10.2210/pdb4qqv/pdb
関連するPDBエントリー2GYS
分子名称Interleukin-3 receptor class 2 subunit beta, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
機能のキーワードintertwined dimer, cytokine receptor, interleukin-3, signaling protein
由来する生物種Mus musculus (mouse)
細胞内の位置Membrane; Single-pass type I membrane protein: P26954
タンパク質・核酸の鎖数4
化学式量合計192678.40
構造登録者
Jackson, C.J.,Young, I.G.,Murphy, J.M.,Carr, P.D.,Ewens, C.L.,Dai, J.,Ollis, D.L. (登録日: 2014-06-30, 公開日: 2014-09-03, 最終更新日: 2024-11-20)
主引用文献Carr, P.D.,Ewens, C.L.,Dai, J.,Ollis, D.L.,Murphy, J.M.,Jackson, C.J.,Young, I.G.
Crystal structure of the mouse interleukin-3 beta-receptor: insights into interleukin-3 binding and receptor activation.
Biochem.J., 463:393-403, 2014
Cited by
PubMed Abstract: Interleukin-3 (IL-3) is a cytokine secreted by mast cells and activated T-cells known to be an important regulator of differentiation, survival, proliferation and activation of a range of haemopoietic lineages. The effects of IL-3 on target cells are mediated by a transmembrane receptor system composed of a cytokine-specific α-subunit and a β-subunit, the principal signalling entity. In the mouse, two β-subunits have co-evolved: a common β-subunit (βc) shared between IL-3 and the related cytokines IL-5 and granulocyte/macrophage colony-stimulating factor (GM-CSF); and an IL-3-specific β-subunit (βIL-3). βIL-3 differs from βc in its specificity for IL-3 and its capacity to bind IL-3 directly in the absence of an α-subunit, and, in the absence of structural information, the basis for these properties has remained enigmatic. In the present study, we have solved the crystal structure of the βIL-3 ectodomain at 3.45 Å (1 Å=0.1 nm) resolution. This structure provides the first evidence that βIL-3 adopts an arch-shaped intertwined homodimer with similar topology to the paralogous βc structure. In contrast with apo-βc, however, the ligand-binding interface of βIL-3 appears to pre-exist in a conformation receptive to IL-3 engagement. Molecular modelling of the IL-3-βIL-3 interface, in conjunction with previous mutational studies, suggests that divergent evolution of both βIL-3 and IL-3 underlies their unique capacity for direct interaction and specificity.
PubMed: 25137390
DOI: 10.1042/BJ20140863
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.45 Å)
構造検証レポート
Validation report summary of 4qqv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-03-05に公開中

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