1J7V
HUMAN IL-10 / IL-10R1 COMPLEX
Summary for 1J7V
| Entry DOI | 10.2210/pdb1j7v/pdb |
| Descriptor | INTERLEUKIN-10, INTERLEUKIN-10 RECEPTOR ALPHA CHAIN (3 entities in total) |
| Functional Keywords | cytokine receptor complex, 4 helix bundle, class 2 receptor, interleukin-10, cytokine-receptor complex, cytokine/receptor |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted: P22301 Membrane; Single-pass type I membrane protein: Q13651 |
| Total number of polymer chains | 2 |
| Total formula weight | 43179.00 |
| Authors | Josephson, K.,Logsdon, N.,Walter, M.R. (deposition date: 2001-05-18, release date: 2001-09-19, Last modification date: 2024-10-30) |
| Primary citation | Josephson, K.,Logsdon, N.J.,Walter, M.R. Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site. Immunity, 15:35-46, 2001 Cited by PubMed Abstract: Interleukin 10 (IL-10) is a dimeric cytokine that plays a central role in suppressing inflammatory responses. These activities are dependent on the interaction of IL-10 with its high-affinity receptor (IL-10R1). This intermediate complex must subsequently recruit the low-affinity IL-10R2 chain before cell signaling can occur. Here we report the 2.9 A crystal structure of IL-10 bound to a soluble form of IL-10R1 (sIL-10R1). The complex consists of two IL-10s and four sIL-10R1 molecules. Several residues in the IL-10/sIL-10R1 interface are conserved in all IL-10 homologs and their receptors. The data suggests that formation of the active IL-10 signaling complex occurs by a novel molecular recognition paradigm where IL-10R1 and IL-10R2 both recognize the same binding site on IL-10. PubMed: 11485736DOI: 10.1016/S1074-7613(01)00169-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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