5EH1

Crystal structure of the extracellular part of receptor 2 of human interferon gamma

5EH1 の概要

• エントリーDOI: 10.2210/pdb5eh1/pdb
• 分子名称: Interferon gamma receptor 2, CYSTEINE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: interferon gamma, immunity, fibronectin iii domain, cytokine
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Single- pass type I membrane protein : P38484
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27269.52

構造登録者

Kolenko, P.,Mikulecky, P.,Zahradnik, J.,Dohnalek, J.,Koval, T.,Cerny, J.,Necasova, I.,Schneider, B. (登録日: 2015-10-27, 公開日: 2016-08-17, 最終更新日: 2024-11-20)

主引用文献

Mikulecky, P.,Zahradnik, J.,Kolenko, P.,Cerny, J.,Charnavets, T.,Kolarova, L.,Necasova, I.,Pham, P.N.,Schneider, B.
Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity.
Acta Crystallogr D Struct Biol, 72:1017-1025, 2016

PubMed Abstract: Interferon-γ receptor 2 is a cell-surface receptor that is required for interferon-γ signalling and therefore plays a critical immunoregulatory role in innate and adaptive immunity against viral and also bacterial and protozoal infections. A crystal structure of the extracellular part of human interferon-γ receptor 2 (IFNγR2) was solved by molecular replacement at 1.8 Å resolution. Similar to other class 2 receptors, IFNγR2 has two fibronectin type III domains. The characteristic structural features of IFNγR2 are concentrated in its N-terminal domain: an extensive π-cation motif of stacked residues KWRWRH, a NAG-W-NAG sandwich (where NAG stands for N-acetyl-D-glucosamine) and finally a helix formed by residues 78-85, which is unique among class 2 receptors. Mass spectrometry and mutational analyses showed the importance of N-linked glycosylation to the stability of the protein and confirmed the presence of two disulfide bonds. Structure-based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon-γ and receptor 1, the ligands of IFNγR2.

PubMed: 27599734
DOI: 10.1107/S2059798316012237

実験手法

X-RAY DIFFRACTION (1.8 Å)