5ixd: Difference between revisions
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==Structure of human JAK1 FERM/SH2 in complex with IFN lambda receptor== | ==Structure of human JAK1 FERM/SH2 in complex with IFN lambda receptor== | ||
<StructureSection load='5ixd' size='340' side='right' caption='[[5ixd]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='5ixd' size='340' side='right'caption='[[5ixd]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ixd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IXD OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5ixd]] 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=5IXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IXD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=5ixd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ixd OCA], [https://pdbe.org/5ixd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ixd RCSB], [https://www.ebi.ac.uk/pdbsum/5ixd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ixd ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5ixd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ixd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Interferon receptor 3D structures|Interferon receptor 3D structures]] | |||
*[[Janus kinase 3D structures|Janus kinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ferrao R]] | ||
[[Category: | [[Category: Lupardus PJ]] | ||
[[Category: | [[Category: Wallweber HJA]] | ||
Latest revision as of 13:36, 6 September 2023
Structure of human JAK1 FERM/SH2 in complex with IFN lambda receptorStructure of human JAK1 FERM/SH2 in complex with IFN lambda receptor
Structural highlights
FunctionJAK1_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. Publication Abstract from PubMedJAK1 is a member of the Janus kinase (JAK) family of non-receptor tyrosine kinases that are activated in response to cytokines and interferons. Here, we present two crystal structures of the human JAK1 FERM and SH2 domains bound to peptides derived from the class II cytokine receptors IFN-lambda receptor 1 and IL-10 receptor 1 (IFNLR1 and IL10RA). These structures reveal an interaction site in the JAK1 FERM that accommodates the so-called "box1" membrane-proximal receptor peptide motif. Biophysical analysis of the JAK1-IFNLR1 interaction indicates that the receptor box1 is the primary driver of the JAK1 interaction, and identifies residues conserved among class II receptors as important for binding. In addition, we demonstrate that a second "box2" receptor motif further stabilizes the JAK1-IFNLR1 complex. Together, these data identify a conserved JAK binding site for receptor peptides and elucidate the mechanism by which class II cytokine receptors interact with JAK1. The Structural Basis for Class II Cytokine Receptor Recognition by JAK1.,Ferrao R, Wallweber HJ, Ho H, Tam C, Franke Y, Quinn J, Lupardus PJ Structure. 2016 Apr 27. pii: S0969-2126(16)30034-X. doi:, 10.1016/j.str.2016.03.023. PMID:27133025[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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