4qqv

Extracellular domains of mouse IL-3 beta receptor

spinqualitylabelsall models 4qqv, resolution 3.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qqv is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.45Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Interleukin receptor 3D structures

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