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Interferon-Inducible Protein 16: Insight into the Interaction with Tumor Suppressor p53

  1. Author:
    Liao, J. C. C.
    Lam, R.
    Brazda, V.
    Duan, S. L.
    Ravichandran, M.
    Ma, J.
    Xiao, T.
    Tempel, W.
    Zuo, X. B.
    Wang, Y. X.
    Chirgadze, N. Y.
    Arrowsmith, C. H.

  2. Author Address

    [Liao, Jack C. C.; Lam, Robert; Duan, Shili; Ma, Justin; Chirgadze, Nickolay Y.; Arrowsmith, Cheryl H.] Univ Hlth Network, Ontario Canc Inst, Campbell Family Canc Res Inst, Toronto, ON M5G 2C4, Canada. [Liao, Jack C. C.; Duan, Shili; Ma, Justin; Arrowsmith, Cheryl H.] Univ Toronto, Dept Med Biophys, Toronto, ON M5G 1L7, Canada. [Lam, Robert; Ravichandran, Mani; Xiao, Ting; Tempel, Wolfram; Arrowsmith, Cheryl H.] Univ Toronto, Struct Genom Consortium, Toronto, ON M5G 1L5, Canada. [Brazda, Vaclav] Acad Sci Czech Republic, Inst Biophys, Vvi, CS-61265 Brno, Czech Republic. [Zuo, Xiaobing; Wang, Yun-Xing] Natl Canc Inst Frederick, Prot Nucle Acid Interact Sect, Struct Biophys Lab, NIH, Frederick, MD 21702 USA. [Chirgadze, Nickolay Y.] Univ Toronto, Dept Pharmacol & Toxicol, Toronto, ON M5S 1A8, Canada.;Arrowsmith, CH, Univ Hlth Network, Ontario Canc Inst, Campbell Family Canc Res Inst, Toronto, ON M5G 2C4, Canada.;carrow@uhnres.utoronto.ca
    1. Year: 2011
    2. Date: Mar
  2. Journal: Structure
    1. 19
    2. 3
    3. Pages: 418-429
  4. Type of Article: Article
  5. ISSN: 0969-2126
  1. Abstract:

    IFI16 is a member of the interferon-inducible HIN-200 family of nuclear proteins. It has been implicated in transcriptional regulation by modulating protein-protein interactions with p53 tumor suppressor protein and other transcription factors. However, the mechanisms of interaction remain unknown. Here, we report the crystal structures of both HIN-A and HIN-B domains of IFI16 determined at 2.0 and 2.35 angstrom resolution, respectively. Each HIN domain comprises a pair of tightly packed OB-fold subdomains that appear to act as a single unit. We show that both HIN domains of IFI16 are capable of enhancing p53-DNA complex formation and transcriptional activation via distinctive means. HIN-A domain binds to the basic C terminus of p53, whereas the HIN-B domain binds to the core DNA-binding region of p53. Both interactions are compatible with the DNA-bound state of p53 and together contribute to the effect of full-length IFI16 on p53-DNA complex formation and transcriptional activation.

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External Sources

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  2. DOI: 10.1016/j.str.2010.12.015
  3. View record in Web of Science®
  4. WOS: 000288689400016

Library Notes

  1. Fiscal Year: FY2010-2011
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