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| ==STRUCTURE OF INTERFERON LAMBDA 1 RECEPTOR WITH HUMAN KINASE JAK1== | | ==STRUCTURE OF INTERFERON LAMBDA 1 RECEPTOR WITH HUMAN KINASE JAK1== |
| <StructureSection load='5l04' size='340' side='right' caption='[[5l04]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5l04' size='340' side='right'caption='[[5l04]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5l04]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L04 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5l04]] is a 2 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=5L04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L04 FirstGlance]. <br> |
| </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></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]] 2.1Å</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=5l04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l04 OCA], [http://pdbe.org/5l04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l04 RCSB], [http://www.ebi.ac.uk/pdbsum/5l04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l04 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=5l04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l04 OCA], [https://pdbe.org/5l04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l04 RCSB], [https://www.ebi.ac.uk/pdbsum/5l04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l04 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/JAK1_HUMAN JAK1_HUMAN]] Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. [[http://www.uniprot.org/uniprot/INLR1_HUMAN INLR1_HUMAN]] The IFNLR1/IL10RB dimer is a receptor for IFNL1, IFNL2 and IFNL3. The ligand/receptor complex seems to signal through the Jak-STAT pathway. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.<ref>PMID:12521379</ref> <ref>PMID:12469119</ref> <ref>PMID:12483210</ref> | | [https://www.uniprot.org/uniprot/JAK1_HUMAN JAK1_HUMAN] Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The crystal structure of a construct consisting of the FERM and SH2-like domains of the human Janus kinase 1 (JAK1) bound to a fragment of the intracellular domain of the interferon-lambda receptor 1 (IFNLR1) has been determined at the nominal resolution of 2.1A. In this structure, the receptor peptide forms an 85-A-long extended chain, in which both the previously identified box1 and box2 regions bind simultaneously to the FERM and SH2-like domains of JAK1. Both domains of JAK1 are generally well ordered, with regions not seen in the crystal structure limited to loops located away from the receptor-binding regions. The structure provides a much more complete and accurate picture of the interactions between JAK1 and IFNLR1 than those given in earlier reports, illuminating the molecular basis of the JAK-cytokine receptor association. A glutamate residue adjacent to the box2 region in IFNLR1 mimics the mode of binding of a phosphotyrosine in classical SH2 domains. It was shown here that a deletion of residues within the box1 region of the receptor abolishes stable interactions with JAK1, although it was previously shown that box2 alone is sufficient to stabilize a similar complex of the interferon-alpha receptor and TYK2.
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| Crystal Structure of a Complex of the Intracellular Domain of Interferon lambda Receptor 1 (IFNLR1) and the FERM/SH2 Domains of Human JAK1.,Zhang D, Wlodawer A, Lubkowski J J Mol Biol. 2016 Nov 20;428(23):4651-4668. doi: 10.1016/j.jmb.2016.10.005. Epub, 2016 Oct 7. PMID:27725180<ref>PMID:27725180</ref>
| | ==See Also== |
| | | *[[Interferon receptor 3D structures|Interferon receptor 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | *[[Janus kinase 3D structures|Janus kinase 3D structures]] |
| </div>
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| <div class="pdbe-citations 5l04" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Non-specific protein-tyrosine kinase]] | | [[Category: Homo sapiens]] |
| [[Category: Lubkowski, J]] | | [[Category: Large Structures]] |
| [[Category: Wlodawer, A]] | | [[Category: Lubkowski J]] |
| [[Category: Zhang, D]] | | [[Category: Wlodawer A]] |
| [[Category: Complex of jak1 and interferon lambda 1]] | | [[Category: Zhang D]] |
| [[Category: Ferm domain]]
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| [[Category: Intracellular domain of ifnlr1]]
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| [[Category: Jak kinase]]
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| [[Category: Sh2-like domain]]
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| [[Category: Transferase-transferase inhibitor complex]]
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