2. Academic Validation
  3. Structural insight into the zinc finger CW domain as a histone modification reader

Structural insight into the zinc finger CW domain as a histone modification reader

  • Structure. 2010 Sep 8;18(9):1127-39. doi: 10.1016/j.str.2010.06.012.
Fahu He 1,  Takashi Umehara,  Kohei Saito,  Takushi Harada,  Satoru Watanabe,  Takashi Yabuki,  Takanori Kigawa,  Mari Takahashi,  Kanako Kuwasako,  Kengo Tsuda,  Takayoshi Matsuda,  Masaaki Aoki,  Eiko Seki,  Naohiro Kobayashi,  Peter Güntert,  Shigeyuki Yokoyama,  Yutaka Muto
Affiliations

Affiliation

  • 1 RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
PMID: 20826339 DOI: 10.1016/j.str.2010.06.012
Abstract

The zinc finger CW (zf-CW) domain is a motif of about 60 residues that is frequently found in proteins involved in epigenetic regulation. Here, we determined the NMR solution structure of the zf-CW domain of the human zf-CW and PWWP domain containing protein 1 (ZCWPW1). The zf-CW domain adopts a new fold in which a zinc ion is coordinated tetrahedrally by four conserved Cys ligand residues. The tertiary structure of the zf-CW domain partially resembles that adopted by the plant homeo domain (PHD) finger bound to the histone tail, suggesting that the zf-CW domain and the PHD finger have similar functions. The solution structure of the complex of the zf-CW domain with the histone H3 tail peptide (1-10) with trimethylated K4 clarified its binding mode. Our structural and biochemical studies have identified the zf-CW domain as a member of the histone modification reader modules for epigenetic regulation.

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