5EH1
Crystal structure of the extracellular part of receptor 2 of human interferon gamma
Summary for 5EH1
| Entry DOI | 10.2210/pdb5eh1/pdb |
| Descriptor | Interferon gamma receptor 2, CYSTEINE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | interferon gamma, immunity, fibronectin iii domain, cytokine |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cell membrane ; Single- pass type I membrane protein : P38484 |
| Total number of polymer chains | 1 |
| Total formula weight | 27269.52 |
| Authors | Kolenko, P.,Mikulecky, P.,Zahradnik, J.,Dohnalek, J.,Koval, T.,Cerny, J.,Necasova, I.,Schneider, B. (deposition date: 2015-10-27, release date: 2016-08-17, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 27599734DOI: 10.1107/S2059798316012237 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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