4DOH
IL20/IL201/IL20R2 Ternary Complex
4DOH の概要
エントリーDOI | 10.2210/pdb4doh/pdb |
分子名称 | Interleukin-20, Interleukin-20 receptor subunit beta, Interleukin-20 receptor subunit alpha, ... (5 entities in total) |
機能のキーワード | il10 family cytokine receptor complex, alpha helical cytokine fold beta sandwhich receptor fold, signaling complex, extracellular, signaling protein |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Secreted: Q9NYY1 Membrane; Single-pass type I membrane protein (By similarity): Q6UXL0 Q9UHF4 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 132994.55 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 22802649DOI: 10.1073/pnas.1117551109 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード