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Crystal Structure of Human Interferon-lambda 1 in Complex with Its High-Affinity Receptor Interferon-lambda R1

  1. Author:
    Miknis, Z. J.
    Magracheva, E.
    Li, W.
    Zdanov, A.
    Kotenko, S. V.
    Wlodawer, A.

  2. Author Address

    [Miknis, Zachary J.; Magracheva, Eugenia; Zdanov, Alexander; Wlodawer, Alexander] NCI Frederick, Macromol Crystallog Lab, Frederick, MD 21702 USA. [Magracheva, Eugenia] SAIC Frederick, Basic Res Program, Frederick, MD 21702 USA. [Li, Wei; Kotenko, Sergei V.] Univ Med & Dent New Jersey, New Jersey Med Sch, Univ Hosp Canc Ctr, Dept Biochem & Mol Biol, Newark, NJ 07103 USA.;Wlodawer, A, NCI Frederick, Macromol Crystallog Lab, Frederick, MD 21702 USA.;wlodawer@nih.gov
    1. Year: 2010
    2. Date: Dec
  2. Journal: Journal of Molecular Biology
    1. 404
    2. 4
    3. Pages: 650-664
  4. Type of Article: Article
  5. ISSN: 0022-2836
  1. Abstract:

    Interferon (IFN)-lambda 1 [also known as interleukiun (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-lambda R1 and IL-10R2. We have determined the structure of human IFN-lambda 1 complexed with human IFN-lambda R1, a receptor unique to type III IFNs. The overall structure of IFN-lambda 1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-lambda R1 consists of two distinct domains having fibronectin type III topology. The ligand receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-lambda R1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it. Published by Elsevier Ltd.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.jmb.2010.09.068
  3. View record in Web of Science®
  4. WOS: 000286018000009

Library Notes

  1. Fiscal Year: FY2010-2011
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