6HGA
Crystal Structure of the human IL-17RC D2-D3-D4 domains in complex with an anti-APP tag Fab
Summary for 6HGA
| Entry DOI | 10.2210/pdb6hga/pdb |
| Related | 6HG4 6HG9 |
| Descriptor | Interleukin-17 receptor C, anti-APP-tag Fab heavy-chain, anti-APP-tag Fab light-chain, ... (5 entities in total) |
| Functional Keywords | fniii domains, fab complex, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 77996.71 |
| Authors | Rondeau, J.M.,Goepfert, A. (deposition date: 2018-08-23, release date: 2020-03-18, Last modification date: 2020-07-29) |
| Primary citation | Goepfert, A.,Lehmann, S.,Blank, J.,Kolbinger, F.,Rondeau, J.M. Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling. Immunity, 52:499-512.e5, 2020 Cited by PubMed Abstract: Interleukin-17A (IL-17A), IL-17F, and IL-17A/F heterodimers are key cytokines of the innate and adaptive immune response. Dysregulation of the IL-17 pathway contributes to immune pathology, and it is therefore important to elucidate the molecular mechanisms that govern IL-17 recognition and signaling. The receptor IL-17RC is thought to act in concert with IL-17RA to transduce IL-17A-, IL-17F-, and IL-17A/F-mediated signals. We report the crystal structure of the extracellular domain of human IL-17RC in complex with IL-17F. In contrast to the expected model, we found that IL-17RC formed a symmetrical 2:1 complex with IL-17F, thus competing with IL-17RA for cytokine binding. Using biophysical techniques, we showed that IL-17A and IL-17A/F also form 2:1 complexes with IL-17RC, suggesting the possibility of IL-17RA-independent IL-17 signaling pathways. The crystal structure of the IL-17RC:IL-17F complex provides a structural basis for IL-17F signaling through IL-17RC, with potential therapeutic applications for respiratory allergy and inflammatory bowel diseases. PubMed: 32187518DOI: 10.1016/j.immuni.2020.02.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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