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Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20

  1. Author:
    Pletnev, S.
    Magracheva, E.
    Kozlov, S.
    Tobin, G.
    Kotenko, S. V.
    Wlodawer, A.
    Zdanov, A.

  2. Author Address

    NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21701 USA NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21701 USA NCI, Canc & Dev Biol Lab, Frederick, MD 21701 USA SAIC Frederick Inc, Basic Res Program, Frederick, MD 21702 USA Biol Mimet Inc, Ft Detrick, MD 21702 USA Univ Med & Dent New Jersey, New Jersey Med Sch, Dept Biochem & Mol Biol, Newark, NJ 07103 USA Zdanov A NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21701 USA
    1. Year: 2003
  2. Journal: Biochemistry
    1. 42
    2. 43
    3. Pages: 12617-12624
  4. Type of Article: Article
  1. Abstract:

    The soluble extracellular domains of human interleukin-20 (IL- 20) receptors I and 11 (sIL-20R1 and sIL20R2), along with their ligands IL-19 and IL-20, were expressed in Drosophila S2 cells and purified to homogeneity. Formation of the receptor/receptor and ligand/receptor complexes was studied by size exclusion chromatography. Both ligands and soluble receptors were found to be monomeric in solution; 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, as well as high-affinity binary complexes with sIL-20R2. Unexpectedly, sIL-20R1 does not bind on its own to either IL-19 or IL-20. Thus, one of the possible consecutive mechanisms of formation of the signaling ternary complex may involve two steps: first, the ligand binds to receptor II, creating a high-affinity binding site for the receptor I, and only then does receptor I complete the complex.

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