This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5eh1
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Current revision
Crystal structure of the extracellular part of receptor 2 of human interferon gamma
| |||||||||||
Categories: Homo sapiens | Large Structures | Cerny J | Dohnalek J | Kolenko P | Koval T | Mikulecky P | Necasova I | Schneider B | Zahradnik J
