Skip NavigationSkip to Content
Return Return to Search Results

Purification of receptor complexes of interleukin-10 - Stoichiometry and the importance of deglycosylation in their crystallization

  1. Author:
    Hoover, D. M.
    Schalk-Hihi, C.
    Chou, C. C.
    Menon, S.
    Wlodawer, A.
    Zdanov, A.

  2. Author Address

    Zdanov A NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Macromol Struct Lab Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Macromol Struct Lab Frederick, MD 21702 USA Schering Plough Res Inst Kenilworth, NJ USA DNAX Res Inst Mol & Cellular Biol Inc, Dept Mol Biol Palo Alto, CA 94304 USA
    1. Year: 1999
  2. Journal: European Journal of Biochemistry
    1. 262
    2. 1
    3. Pages: 134-141
  4. Type of Article: Article
  1. Abstract:

    Interleukin-10 (IL-10) is a pleiotropic immunosuppressive cytokine that has a wide range of effects in controlling inflammatory responses. Viral IL-10 (vIL-10) is a homologue of human IL-IO (hIL-10) produced by Epstein-Barr virus (EBV). Both hIL-10 and vIL-10 bind to the soluble extracellular fragment of the cytokine receptor IL-10R1 (shIL-10R1). The stoichiometry of the vIL-10: shIL-10R1 complex has been found to be the same as hIL-10 : shIL-10R1, with two vIL-10 dimers binding to four shIL-10R1 monomers. Complexes of both hIL-10 and vIL-10 with glycosylated shIL-10R1 could not be crystallized. Controlled deglycosylation using peptide: N-glycosidase F and endo-beta-N-acetylglucosaminidase F-3 resulted in the formation of crystals of both hIL-10 : shIL-10R1 and vIL-10 : shIL-10R1 complexes, indicating that the difficulty in the crystal formation was largely due to the presence of complex carbohydrate side chains. The availability of the structure of the ligand-receptor complexes should facilitate our understanding of the basis of the interaction between IL-10 and the IL-10 receptor. [References: 28]

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel