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TitleOrganizing structural principles of the IL-17 ligand-receptor axis.
Journal, issue, pagesNature, Vol. 609, Issue 7927, Page 622-629, Year 2022
Publish dateJul 21, 2022
AuthorsSteven C Wilson / Nathanael A Caveney / Michelle Yen / Christoph Pollmann / Xinyu Xiang / Kevin M Jude / Maximillian Hafer / Naotaka Tsutsumi / Jacob Piehler / K Christopher Garcia /
PubMed AbstractThe IL-17 family of cytokines and receptors have central roles in host defence against infection and development of inflammatory diseases. The compositions and structures of functional IL-17 family ...The IL-17 family of cytokines and receptors have central roles in host defence against infection and development of inflammatory diseases. The compositions and structures of functional IL-17 family ligand-receptor signalling assemblies remain unclear. IL-17E (also known as IL-25) is a key regulator of type 2 immune responses and driver of inflammatory diseases, such as allergic asthma, and requires both IL-17 receptor A (IL-17RA) and IL-17RB to elicit functional responses. Here we studied IL-25-IL-17RB binary and IL-25-IL-17RB-IL-17RA ternary complexes using a combination of cryo-electron microscopy, single-molecule imaging and cell-based signalling approaches. The IL-25-IL-17RB-IL-17RA ternary signalling assembly is a C2-symmetric complex in which the IL-25-IL-17RB homodimer is flanked by two 'wing-like' IL-17RA co-receptors through a 'tip-to-tip' geometry that is the key receptor-receptor interaction required for initiation of signal transduction. IL-25 interacts solely with IL-17RB to allosterically promote the formation of the IL-17RB-IL-17RA tip-to-tip interface. The resulting large separation between the receptors at the membrane-proximal level may reflect proximity constraints imposed by the intracellular domains for signalling. Cryo-electron microscopy structures of IL-17A-IL-17RA and IL-17A-IL-17RA-IL-17RC complexes reveal that this tip-to-tip architecture is a key organizing principle of the IL-17 receptor family. Furthermore, these studies reveal dual actions for IL-17RA sharing among IL-17 cytokine complexes, by either directly engaging IL-17 cytokines or alternatively functioning as a co-receptor.
External linksNature / PubMed:35863378 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 4.4 Å
Structure data

26833

7uwj

EMDB-26833, PDB-7uwj:
Structure of the homodimeric IL-25-IL-17RB binary complex
Method: EM (single particle) / Resolution: 3.2 Å

26834

7uwk

EMDB-26834, PDB-7uwk:
Structure of the higher-order IL-25-IL-17RB complex
Method: EM (single particle) / Resolution: 4.4 Å

26835

7uwl

EMDB-26835, PDB-7uwl:
Structure of the IL-25-IL-17RB-IL-17RA ternary complex
Method: EM (single particle) / Resolution: 3.7 Å

26836

7uwm

EMDB-26836, PDB-7uwm:
Structure of the IL-17A-IL-17RA binary complex
Method: EM (single particle) / Resolution: 2.5 Å

26837

7uwn

EMDB-26837, PDB-7uwn:
Structure of the IL-17A-IL-17RA-IL-17RC ternary complex
Method: EM (single particle) / Resolution: 3.01 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
KeywordsCYTOKINE / Receptor complex / IL-17E / IL-25 / IL-17RB / IL-17RA / IL-17A / IL-17RC

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