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Crystal Structure of Epstein-Barr Virus Protein Bcrf1, a Homolog of Cellular Interleukin-10

  1. Author:
    Zdanov, A.
    Schalkhihi, C.
    Menon, S.
    Moore, K. W.
    Wlodawer, A.

  2. Author Address

    Wlodawer A NCI MACROMOL STRUCT LAB FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM FREDERICK, MD 21702 USA NCI MACROMOL STRUCT LAB FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM FREDERICK, MD 21702 USA DNAX RES INST MOL & CELLULAR BIOL INC DEPT MOL BIOL PALO ALTO, CA 94304 USA
    1. Year: 1997
  2. Journal: Journal of Molecular Biology
    1. 268
    2. 2
    3. Pages: 460-467
  4. Type of Article: Article
  1. Abstract:

    The crystal structure of Epstein-Barr virus protein BCRF1, an analog of cellular interleukin-10 (IL-10), has been determined at the resolution of 1.9 Angstrom and refined to an R-factor 0.191. The structure of this cytokine is similar to that of human IL-10 (hIL-10), forming an intercalated dimer of two 17 kDa polypeptides related by a crystallographic 2-fold symmetry axis. BCRF1 exhibits novel conformations of the N-terminal coil and of the loop between helices A and B compared to hIL-10. These regions are likely to be involved in binding of one or more components of the IL-10 receptor system, and thus the structural differences may account for the lower binding affinity and limited spectrum of biological activities of viral IL-10, compared to hIL-10. (C) 1997 Academic Press Limited. [References: 27]

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