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| | ==Crystal structure of human Interleukin-5 in complex with its alpha receptor== | | ==Crystal structure of human Interleukin-5 in complex with its alpha receptor== |
| - | <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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VA2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3va2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IL5RA, IL5R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IL5RA, IL5R ([https://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3va2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3va2 OCA], [http://pdbe.org/3va2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3va2 RCSB], [http://www.ebi.ac.uk/pdbsum/3va2 PDBsum], [http://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> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IL5_HUMAN IL5_HUMAN]] Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. [[http://www.uniprot.org/uniprot/IL5RA_HUMAN IL5RA_HUMAN]] This is the receptor for interleukin-5. The alpha chain binds to IL5. | + | [[https://www.uniprot.org/uniprot/IL5_HUMAN IL5_HUMAN]] Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. [[https://www.uniprot.org/uniprot/IL5RA_HUMAN IL5RA_HUMAN]] This is the receptor for interleukin-5. The alpha chain binds to IL5. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Interleukin|Interleukin]] | + | *[[Interleukin 3D structures|Interleukin 3D structures]] |
| - | *[[Interleukin receptor|Interleukin receptor]] | + | *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Kukimoto-Niino, M]] | | [[Category: Kukimoto-Niino, M]] |
| | [[Category: Kusano, S]] | | [[Category: Kusano, S]] |
| Structural highlights
Function
[IL5_HUMAN] Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. [IL5RA_HUMAN] This is the receptor for interleukin-5. The alpha chain binds to IL5.
Publication Abstract from PubMed
Interleukin-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 Also
References
- ↑ Kusano S, Kukimoto-Niino M, Hino N, Ohsawa N, Ikutani M, Takaki S, Sakamoto K, Hara-Yokoyama M, Shirouzu M, Takatsu K, Yokoyama S. Structural basis of interleukin-5 dimer recognition by its alpha receptor. Protein Sci. 2012 Jun;21(6):850-64. doi: 10.1002/pro.2072. Epub 2012 Apr 23. PMID:22528658 doi:10.1002/pro.2072
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