Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality

Takashi Matsui, Yoshio Kodera, Emi Miyauchi, Hidekazu Tanaka, Hiroshi Endoh, Hiroyoshi Komatsu, Takeshi Tanaka, Toshiyuki Kohno, Tadakazu Maeda

    Research output: Contribution to journalArticlepeer-review

    9 Citations (Scopus)


    Nucleocapsid protein of HIV, containing two CCHC-type zinc fingers connected by a linker, is a multi-functional protein involved in many critical steps of the HIV life cycle. Several in vitro investigations demonstrated that the reactivities of the first zinc finger flanked by the linker of HIV-1 NCp7 and HIV-2 NCp8 were essential for binding to viral RNA, however, that of the second zinc finger flanked by the linker of NCp7 was very weak and non-specific, whereas the part of NCp8 called NCp8-f2, interacted strongly and specifically with viral RNA. In this study, the three-dimensional structure of NCp8-f2 was determined for the first time. Furthermore, we established that NCp8-f2 specifically binds to the stem-loop SD in viral RNA, and that the hydrophobic cleft and the basic residues close to the cleft were essential for specific binding to SD. We discuss the functional significance of NCp8-f2 for NCp8 being a multi-functional protein.

    Original languageEnglish
    Pages (from-to)673-678
    Number of pages6
    JournalBiochemical and biophysical research communications
    Issue number3
    Publication statusPublished - 2007 Jul 6


    • 2D NMR
    • HIV
    • Nucleocapsid protein
    • RNA binding protein
    • Zinc finger

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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