4DOH

IL20/IL201/IL20R2 Ternary Complex

Summary for 4DOH

• Entry DOI: 10.2210/pdb4doh/pdb
• Descriptor: Interleukin-20, Interleukin-20 receptor subunit beta, Interleukin-20 receptor subunit alpha, ... (5 entities in total)
• Functional Keywords: il10 family cytokine receptor complex, alpha helical cytokine fold beta sandwhich receptor fold, signaling complex, extracellular, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: Q9NYY1; Membrane; Single-pass type I membrane protein (By similarity): Q6UXL0 Q9UHF4
• Total number of polymer chains: 6
• Total formula weight: 132994.55

Authors

Logsdon, N.J.,Walter, M.R. (deposition date: 2012-02-09, release date: 2012-07-18, Last modification date: 2024-11-20)

Primary citation

Logsdon, N.J.,Deshpande, A.,Harris, B.D.,Rajashankar, K.R.,Walter, M.R.
Structural basis for receptor sharing and activation by interleukin-20 receptor-2 (IL-20R2) binding cytokines.
Proc.Natl.Acad.Sci.USA, 109:12704-12709, 2012

PubMed Abstract: Interleukin 20 (IL-20) is a pleotropic IL-10 family cytokine that protects epithelial surfaces from pathogens. However, dysregulated IL-20 signaling is implicated in several human pathologies including psoriasis, rheumatoid arthritis, atherosclerosis, and osteoporosis. IL-20, and related cytokines IL-19 and IL-24, designated IL-20 subfamily cytokines (IL-20SFCs), induce cellular responses through an IL-20R1/IL-20R2 (type I) receptor heterodimer, whereas IL-20 and IL-24 also signal through the IL-22R1/IL-20R2 (type II) receptor complex. The crystal structure of the IL-20/IL-20R1/IL-20R2 complex reveals how type I and II complexes discriminate cognate from noncognate ligands. The structure also defines how the receptor-cytokine interfaces are affinity tuned to allow distinct signaling through a receptor complex shared by three different ligands. Our results provide unique insights into the complexity of IL-20SFC signaling that may be critical in the design of mechanistic-based inhibitors of IL-20SFC-mediated inflammatory disease.

PubMed: 22802649
DOI: 10.1073/pnas.1117551109

Experimental method

X-RAY DIFFRACTION (2.8 Å)