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PDBsum entry 2ers

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Signaling protein PDB id
2ers
Contents
Protein chain
66 a.a.

References listed in PDB file
Key reference
Title The structure of the interleukin-15 alpha receptor and its implications for ligand binding.
Authors I.Lorenzen, A.J.Dingley, Y.Jacques, J.Grötzinger.
Ref. J Biol Chem, 2006, 281, 6642-6647. [DOI no: 10.1074/jbc.M513118200]
PubMed id 16377614
Abstract
Interleukin (IL)-15 is a member of the small four alpha-helix bundle family of cytokines. IL-15 was discovered by its ability to mimic IL-2-mediated T-cell proliferation. Both cytokines share the beta and gamma receptor chains of the IL-2 receptor for signal transduction. However, in addition, they target specific alpha chain receptors IL-15Ralpha and IL-2Ralpha, respectively. The exceptionally high affinity binding of IL-15 to IL-15Ralpha is mediated by its sushi domain. Here we present the solution structure of the IL-15Ralpha sushi domain solved by NMR spectroscopy and a model of its complex with IL-15. The model shows that, rather than the familiar hydrophobic forces dominating the interaction interface between cytokines and their cognate receptors, the interaction between the IL-15 and IL-15Ralpha complex involves a large network of ionic interactions. This type of interaction explains the exceptionally high affinity of the IL-15.IL-15Ralpha complex, which is essential for the biological effects of this important cytokine and which is not observed in other cytokine/cytokine receptor complexes.
Figure 2.
The structure of the sushi domain of the IL-15Rα. A, ribbon representation of the average energy-minimized structure. The two disulfide bonds are yellow, and the N and C termini are labeled. B, stereo view of 20 superimposed structures in spaghetti representation and generated by distance geometry calculations, N and C denotes the N and C termini, respectively.
Figure 4.
Model of the IL-15 with its α receptor sushi domain as ribbon representation. A, model of the complex of the sushi domain (blue) and an IL-15 model (yellow). B, the proposed binding interface between IL-15 and IL-15Rα.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 6642-6647) copyright 2006.
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