Characterization of the Recombinant Extracellular Domains of Human Interleukin-20 Receptors and Their Complexes with Interleukin-19 and Interleukin-20

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• 作者：Sergei Pletnev ; Eugenia Magracheva ; Serguei Kozlov ; Gregory Tobin ; Sergei V. Kotenko ; Alexander Wlodawer ; and Alexander Zdanov
• 刊名：Biochemistry
• 出版年：2003
• 出版时间：November 4, 2003
• 年：2003
• 卷：42
• 期：43
• 页码：12617 - 12624
• 全文大小：198K
• 年卷期：v.42,no.43(November 4, 2003)
• ISSN：1520-4995

文摘

The soluble extracellular domains of human interleukin-20 (IL-20) receptors I and II (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells andpurified to homogeneity. Formation of the receptor/receptor and ligand/receptor complexes was studiedby size exclusion chromatography. Both ligands and soluble receptors were found to be monomeric insolution; homo- or heterodimers are not formed even at elevated concentrations. Under native conditions,both IL-19 and IL-20 form stable ternary 1:1:1 complexes with the sIL-20R1 and sIL20R2 receptors, aswell as high-affinity binary complexes with sIL-20R2. Unexpectedly, sIL-20R1 does not bind on its ownto either IL-19 or IL-20. Thus, one of the possible consecutive mechanisms of formation of the signalingternary complex may involve two steps: first, the ligand binds to receptor II, creating a high-affinitybinding site for the receptor I, and only then does receptor I complete the complex.