5eh1: Difference between revisions
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The entry | ==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=''> | |||
== Structural highlights == | |||
<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='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='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'>[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> | |||
== Disease == | |||
[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 == | |||
[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;"> | |||
== 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<ref>PMID:27599734</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5eh1" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Cerny J]] | |||
[[Category: Dohnalek J]] | |||
[[Category: Kolenko P]] | |||
[[Category: Koval T]] | |||
[[Category: Mikulecky P]] | |||
[[Category: Necasova I]] | |||
[[Category: Schneider B]] | |||
[[Category: Zahradnik J]] | |||
Latest revision as of 09:26, 5 July 2023
Crystal structure of the extracellular part of receptor 2 of human interferon gammaCrystal structure of the extracellular part of receptor 2 of human interferon gamma
Structural highlights
DiseaseINGR2_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. FunctionINGR2_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 PubMedInterferon-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 AlsoReferences
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