title: Structural insight into the zinc finger CW domain as a histone modification reader.
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.
authors.affiliation: RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
authors.forename: Fahu
authors.initials: F
authors.lastname: He
authors.forename: Takashi
authors.initials: T
authors.lastname: Umehara
authors.forename: Kohei
authors.initials: K
authors.lastname: Saito
authors.forename: Takushi
authors.initials: T
authors.lastname: Harada
authors.forename: Satoru
authors.initials: S
authors.lastname: Watanabe
authors.forename: Takashi
authors.initials: T
authors.lastname: Yabuki
authors.forename: Takanori
authors.initials: T
authors.lastname: Kigawa
authors.forename: Mari
authors.initials: M
authors.lastname: Takahashi
authors.forename: Kanako
authors.initials: K
authors.lastname: Kuwasako
authors.forename: Kengo
authors.initials: K
authors.lastname: Tsuda
authors.forename: Takayoshi
authors.initials: T
authors.lastname: Matsuda
authors.forename: Masaaki
authors.initials: M
authors.lastname: Aoki
authors.forename: Eiko
authors.initials: E
authors.lastname: Seki
authors.forename: Naohiro
authors.initials: N
authors.lastname: Kobayashi
authors.forename: Peter
authors.initials: P
authors.lastname: Güntert
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Muto
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D044127:Epigenesis, Genetic; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D016335:Zinc Fingers
chemical_list: D006657:Histones