Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution

Maki S. Tawaramoto, Sam Yong Park, Yoshinori Tanaka, Osamu Nureki, Hitoshi Kurumizaka, Shigeyuki Yokoyama

    Research output: Contribution to journalArticle

    10 Citations (Scopus)

    Abstract

    The human centromere protein B (CENP-B), a centromeric heterochromatin component, forms a homodimer that specifically binds to a distinct DNA sequence (the CENP-B box), which appears within every other α-satellite repeat. Previously, we determined the structure of the human CENP-B DNA-binding domain, CENP-B-(1-129), complexed with the CENP-B box DNA. In the present study, we determined the crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-Å resolution. CENP-B-(540-599) contains two α-helices, which are folded into an antiparallel configuration. The CENP-B-(540-599) dimer formed a symmetrical, antiparallel, four-helix bundle structure with a large hydrophobic patch in which 23 residues of one monomer form van der Waals contacts with the other monomer. In the CENP-B-(540-599) dimer, the N-terminal ends of CENP-B-(540-599) are oriented on opposite sides of the dimer. This CENP-B dimer configuration may be suitable for capturing two distant CENP-B boxes during centromeric heterochromatin formation.

    Original languageEnglish
    Pages (from-to)51454-51461
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume278
    Issue number51
    DOIs
    Publication statusPublished - 2003 Dec 19

    Fingerprint

    Centromere Protein B
    Protein Multimerization
    Dimerization
    Crystal structure
    Dimers
    Heterochromatin
    human CENPB protein
    Monomers
    DNA sequences
    DNA

    ASJC Scopus subject areas

    • Biochemistry

    Cite this

    Tawaramoto, M. S., Park, S. Y., Tanaka, Y., Nureki, O., Kurumizaka, H., & Yokoyama, S. (2003). Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution. Journal of Biological Chemistry, 278(51), 51454-51461. https://doi.org/10.1074/jbc.M310388200

    Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution. / Tawaramoto, Maki S.; Park, Sam Yong; Tanaka, Yoshinori; Nureki, Osamu; Kurumizaka, Hitoshi; Yokoyama, Shigeyuki.

    In: Journal of Biological Chemistry, Vol. 278, No. 51, 19.12.2003, p. 51454-51461.

    Research output: Contribution to journalArticle

    Tawaramoto, MS, Park, SY, Tanaka, Y, Nureki, O, Kurumizaka, H & Yokoyama, S 2003, 'Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution', Journal of Biological Chemistry, vol. 278, no. 51, pp. 51454-51461. https://doi.org/10.1074/jbc.M310388200
    Tawaramoto, Maki S. ; Park, Sam Yong ; Tanaka, Yoshinori ; Nureki, Osamu ; Kurumizaka, Hitoshi ; Yokoyama, Shigeyuki. / Crystal Structure of the Human Centromere Protein B (CENP-B) Dimerization Domain at 1.65-Å Resolution. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 51. pp. 51454-51461.
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