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Crystal structure of interleukin-19 defines a new subfamily of helical cytokines

  1. Author:
    Chang, C. S.
    Magracheva, E.
    Kozlov, S.
    Fong, S.
    Tobin, G.
    Kotenko, S.
    Wlodawer, A.
    Zdanov, A.

  2. Author Address

    NCI, Ctr Canc Res, Macromol Crystallog Lab, Prot Struct Sect,NIH, POB B, Frederick, MD 21702 USA NCI, Ctr Canc Res, Macromol Crystallog Lab, Prot Struct Sect,NIH, Frederick, MD 21702 USA SAIC Frederick Inc, Intramural Res Support Program, Frederick, MD 21702 USA NCI, Canc & Dev Biol Lab, NIH, Frederick, MD 21702 USA Univ Med & Dent New Jersey, New Jersey Med Sch, Dept Biochem & Mol Biol, Newark, NJ 07103 USA Zdanov A NCI, Ctr Canc Res, Macromol Crystallog Lab, Prot Struct Sect,NIH, POB B, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Journal of Biological Chemistry
    1. 278
    2. 5
    3. Pages: 3308-3313
  4. Type of Article: Article
  1. Abstract:

    Interleukin-19 (IL-19) is a novel cytokine that was initially identified during a sequence data base search aimed at finding potential IL-10 homologs. IL-19 shares a receptor complex with IL-20, indicating that the biological activities of these two cytokines overlap and that both may play an important role in regulating development and proper functioning of the skin. We determined the crystal structure of human recombinant IL-19 and refined it at 1.95-Angstrom resolution to an R-factor of 0.157. Unlike IL-10, which forms an intercalated dimer, the molecule of IL-19 is a monomer made of seven amphipathic helices, A-G, creating a unique helical bundle. On the basis of the observed structure, we propose that IL-19, IL-20, and other putative members of the proposed IL-10 family together form a distinct subfamily of helical cytokines.

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