2ERS
Solution structure of the Interleukin-15 receptor sushi domain
Summary for 2ERS
| Entry DOI | 10.2210/pdb2ers/pdb |
| NMR Information | BMRB: 6882 |
| Descriptor | Interleukin-15 receptor alpha chain (1 entity in total) |
| Functional Keywords | sushi domain, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein. Isoform 5: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Isoform 6: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Isoform 7: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Isoform 8: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Soluble interleukin-15 receptor subunit alpha: Secreted, extracellular space: Q13261 |
| Total number of polymer chains | 1 |
| Total formula weight | 7473.59 |
| Authors | Lorenzen, I.,Dingley, A.J.,Grotzinger, J. (deposition date: 2005-10-25, release date: 2006-02-07, Last modification date: 2024-10-16) |
| Primary citation | Lorenzen, I.,Dingley, A.J.,Jacques, Y.,Grotzinger, J. The structure of the interleukin-15 alpha receptor and its implications for ligand binding. J.Biol.Chem., 281:6642-6647, 2006 Cited by PubMed 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. PubMed: 16377614DOI: 10.1074/jbc.M513118200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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