5ixd: Difference between revisions

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<StructureSection load='5ixd' size='340' side='right'caption='[[5ixd]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='5ixd' size='340' side='right'caption='[[5ixd]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ixd]] is a 2 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=5IXD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IXD FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 2.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ixi|5ixi]]</td></tr>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JAK1, JAK1A, JAK1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IFNLR1, IL28RA, LICR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ixd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ixd OCA], [http://pdbe.org/5ixd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ixd RCSB], [http://www.ebi.ac.uk/pdbsum/5ixd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ixd 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Non-specific protein-tyrosine kinase]]
[[Category: Ferrao R]]
[[Category: Ferrao, R]]
[[Category: Lupardus PJ]]
[[Category: Lupardus, P J]]
[[Category: Wallweber HJA]]
[[Category: Wallweber, H J.A]]
[[Category: Cytokine]]
[[Category: Ifnlr1]]
[[Category: Interferon]]
[[Category: Jak kinase]]
[[Category: Jak1]]

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

5ixd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Publication Abstract from PubMed

JAK1 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 Also

References

  1. ↑ Ferrao R, Wallweber HJ, Ho H, Tam C, Franke Y, Quinn J, Lupardus PJ. The Structural Basis for Class II Cytokine Receptor Recognition by JAK1. Structure. 2016 Apr 27. pii: S0969-2126(16)30034-X. doi:, 10.1016/j.str.2016.03.023. PMID:27133025 doi:http://dx.doi.org/10.1016/j.str.2016.03.023

5ixd, resolution 2.85Å

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