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| | <StructureSection load='4qqv' size='340' side='right'caption='[[4qqv]], [[Resolution|resolution]] 3.45Å' scene=''> | | <StructureSection load='4qqv' size='340' side='right'caption='[[4qqv]], [[Resolution|resolution]] 3.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qqv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qqv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gys|2gys]]</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=4qqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqv OCA], [https://pdbe.org/4qqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqv RCSB], [https://www.ebi.ac.uk/pdbsum/4qqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ai2ca, Csf2rb2, Il3r, Il3rb2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4qqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqv OCA], [http://pdbe.org/4qqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qqv RCSB], [http://www.ebi.ac.uk/pdbsum/4qqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IL3B2_MOUSE IL3B2_MOUSE]] In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. | + | [https://www.uniprot.org/uniprot/IL3B2_MOUSE IL3B2_MOUSE] In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. |
| | <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 receptor|Interleukin receptor]] | + | *[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Carr, P D]] | + | [[Category: Carr PD]] |
| - | [[Category: Dai, J]] | + | [[Category: Dai J]] |
| - | [[Category: Ewens, C L]] | + | [[Category: Ewens CL]] |
| - | [[Category: Jackson, C J]] | + | [[Category: Jackson CJ]] |
| - | [[Category: Murphy, J M]] | + | [[Category: Murphy JM]] |
| - | [[Category: Ollis, D L]] | + | [[Category: Ollis DL]] |
| - | [[Category: Young, I G]] | + | [[Category: Young IG]] |
| - | [[Category: Cytokine receptor]]
| + | |
| - | [[Category: Interleukin-3]]
| + | |
| - | [[Category: Intertwined dimer]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
IL3B2_MOUSE In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors.
Publication Abstract from PubMed
Interleukin-3 (IL-3) is a cytokine secreted by mast cells and activated T-cells known to be an important regulator of differentiation, survival, proliferation and activation of a range of hematopoietic lineages. The effects of IL-3 on target cells are mediated by a transmembrane receptor system composed of a cytokine-specific alpha-subunit and a beta-subunit, the principal signalling entity. In the mouse, two beta-subunits have co-evolved: a common beta-subunit (betac) shared between IL-3 and the related cytokines, IL-5 and GM-CSF; and an IL-3-specific beta-subunit (betaIL-3). betaIL3 differs from betac in its specificity for IL-3 and its capacity to bind IL-3 directly in the absence of an alpha-subunit and, in the absence of structural information, the basis for these properties has remained enigmatic. Here, we present the crystal structure of the betaIL-3 ectodomain at 3.45 A resolution. This structure provides the first evidence that betaIL-3 adopts an arch-shaped, intertwined homodimer with similar topology to the paralogous betac structure. In contrast to apo-betac, however, the ligand-binding interface of betaIL3 appears to pre-exist in a conformation receptive to IL-3 engagement. Molecular modelling of the IL-3:betaIL3 interface, in conjunction with previous mutational studies, suggests that divergent evolution of both betaIL3 and IL-3 underlies their unique capacity for direct interaction and specificity.
Crystal structure of the mouse interleukin-3 beta-receptor: insights into interleukin3 binding and receptor activation.,Carr PD, Ewens CL, Dai J, Ollis DL, Murphy JM, Jackson CJ, Young IG Biochem J. 2014 Aug 19. PMID:25137390[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carr PD, Ewens CL, Dai J, Ollis DL, Murphy JM, Jackson CJ, Young IG. Crystal structure of the mouse interleukin-3 beta-receptor: insights into interleukin3 binding and receptor activation. Biochem J. 2014 Aug 19. PMID:25137390 doi:http://dx.doi.org/10.1042/BJ20140863
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