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| | ==Crystal structure of the extracellular part of receptor 2 of human interferon gamma== | | ==Crystal structure of the extracellular part of receptor 2 of human interferon gamma== |
| - | <StructureSection load='5eh1' size='340' side='right' caption='[[5eh1]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5eh1' size='340' side='right'caption='[[5eh1]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5eh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5eh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EH1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IFNGR2, IFNGT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eh1 OCA], [http://pdbe.org/5eh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eh1 RCSB], [http://www.ebi.ac.uk/pdbsum/5eh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eh1 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5eh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eh1 OCA], [https://pdbe.org/5eh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5eh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eh1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN]] Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN] Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN]] Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114).<ref>PMID:15356148</ref> <ref>PMID:7615558</ref> <ref>PMID:7673114</ref> <ref>PMID:8124716</ref> | + | [https://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN] Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114).<ref>PMID:15356148</ref> <ref>PMID:7615558</ref> <ref>PMID:7673114</ref> <ref>PMID:8124716</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Interferon receptor|Interferon receptor]] | + | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Cerny, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Dohnalek, J]] | + | [[Category: Cerny J]] |
| - | [[Category: Kolenko, P]] | + | [[Category: Dohnalek J]] |
| - | [[Category: Koval, T]] | + | [[Category: Kolenko P]] |
| - | [[Category: Mikulecky, P]] | + | [[Category: Koval T]] |
| - | [[Category: Necasova, I]] | + | [[Category: Mikulecky P]] |
| - | [[Category: Schneider, B]] | + | [[Category: Necasova I]] |
| - | [[Category: Zahradnik, J]] | + | [[Category: Schneider B]] |
| - | [[Category: Cytokine]]
| + | [[Category: Zahradnik J]] |
| - | [[Category: Fibronectin iii domain]]
| + | |
| - | [[Category: Immunity]]
| + | |
| - | [[Category: Interferon gamma]]
| + | |
| Structural highlights
Disease
INGR2_HUMAN Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.
Function
INGR2_HUMAN Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114).[1] [2] [3] [4]
Publication Abstract from PubMed
Interferon-gamma receptor 2 is a cell-surface receptor that is required for interferon-gamma 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-gamma receptor 2 (IFNgammaR2) was solved by molecular replacement at 1.8 A resolution. Similar to other class 2 receptors, IFNgammaR2 has two fibronectin type III domains. The characteristic structural features of IFNgammaR2 are concentrated in its N-terminal domain: an extensive pi-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-gamma and receptor 1, the ligands of IFNgammaR2.
Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity.,Mikulecky P, Zahradnik J, Kolenko P, Cerny J, Charnavets T, Kolarova L, Necasova I, Pham PN, Schneider B Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):1017-25. doi:, 10.1107/S2059798316012237. Epub 2016 Aug 18. PMID:27599734[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rosenzweig SD, Schwartz OM, Brown MR, Leto TL, Holland SM. Characterization of a dipeptide motif regulating IFN-gamma receptor 2 plasma membrane accumulation and IFN-gamma responsiveness. J Immunol. 2004 Sep 15;173(6):3991-9. PMID:15356148
- ↑ Sakatsume M, Igarashi K, Winestock KD, Garotta G, Larner AC, Finbloom DS. The Jak kinases differentially associate with the alpha and beta (accessory factor) chains of the interferon gamma receptor to form a functional receptor unit capable of activating STAT transcription factors. J Biol Chem. 1995 Jul 21;270(29):17528-34. PMID:7615558
- ↑ Kotenko SV, Izotova LS, Pollack BP, Mariano TM, Donnelly RJ, Muthukumaran G, Cook JR, Garotta G, Silvennoinen O, Ihle JN, et al.. Interaction between the components of the interferon gamma receptor complex. J Biol Chem. 1995 Sep 8;270(36):20915-21. PMID:7673114
- ↑ Soh J, Donnelly RJ, Kotenko S, Mariano TM, Cook JR, Wang N, Emanuel S, Schwartz B, Miki T, Pestka S. Identification and sequence of an accessory factor required for activation of the human interferon gamma receptor. Cell. 1994 Mar 11;76(5):793-802. PMID:8124716
- ↑ Mikulecky P, Zahradnik J, Kolenko P, Cerny J, Charnavets T, Kolarova L, Necasova I, Pham PN, Schneider B. Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity. Acta Crystallogr D Struct Biol. 2016 Sep;72(Pt 9):1017-25. doi:, 10.1107/S2059798316012237. Epub 2016 Aug 18. PMID:27599734 doi:http://dx.doi.org/10.1107/S2059798316012237
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