3va2: Difference between revisions
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<StructureSection load='3va2' size='340' side='right'caption='[[3va2]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3va2' size='340' side='right'caption='[[3va2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3va2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3va2]] is a 3 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=3VA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VA2 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]] 2.703Å</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=3va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3va2 OCA], [https://pdbe.org/3va2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3va2 RCSB], [https://www.ebi.ac.uk/pdbsum/3va2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3va2 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=3va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3va2 OCA], [https://pdbe.org/3va2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3va2 RCSB], [https://www.ebi.ac.uk/pdbsum/3va2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3va2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kukimoto-Niino | [[Category: Kukimoto-Niino M]] | ||
[[Category: Kusano | [[Category: Kusano S]] | ||
[[Category: Shirouzu | [[Category: Shirouzu M]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 05:33, 21 November 2024
Crystal structure of human Interleukin-5 in complex with its alpha receptorCrystal structure of human Interleukin-5 in complex with its alpha receptor
Structural highlights
Publication Abstract from PubMedInterleukin-5 (IL-5), a major hematopoietin, stimulates eosinophil proliferation, migration, and activation, which have been implicated in the pathogenesis of allergic inflammatory diseases, such as asthma. The specific IL-5 receptor (IL-5R) consists of the IL-5 receptor alpha subunit (IL-5RA) and the common receptor beta subunit (betac). IL-5 binding to IL-5R on target cells induces rapid tyrosine phosphorylation and activation of various cellular proteins, including JAK1/JAK2 and STAT1/STAT5. Here, we report the crystal structure of dimeric IL-5 in complex with the IL-5RA extracellular domains. The structure revealed that IL-5RA sandwiches the IL-5 homodimer by three tandem domains, arranged in a "wrench-like" architecture. This association mode was confirmed for human cells expressing IL-5 and the full-length IL-5RA by applying expanded genetic code technology: protein photo-cross-linking experiments revealed that the two proteins interact with each other in vivo in the same manner as that in the crystal structure. Furthermore, a comparison with the previously reported, partial GM-CSF*GM-CSFRA*betac structure enabled us to propose complete structural models for the IL-5 and GM-CSF receptor complexes, and to identify the residues conferring the cytokine-specificities of IL-5RA and GM-CSFRA. Structural basis of interleukin-5 dimer recognition by its alpha receptor.,Kusano S, Kukimoto-Niino M, Hino N, Ohsawa N, Ikutani M, Takaki S, Sakamoto K, Hara-Yokoyama M, Shirouzu M, Takatsu K, Yokoyama S Protein Sci. 2012 Jun;21(6):850-64. doi: 10.1002/pro.2072. Epub 2012 Apr 23. PMID:22528658[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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