| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2029768 | Structure | 2010 | 13 Pages |
SummaryThe 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.
► This is the first solution structure for zf-CW domain as a novel zinc finger ► Preference and binding affinities between zf-CW and H3K4me have been determined ► The first complex structure of zf-CW-H3K4me3 showed a novel binding mode ► The zf-CW domain was identified as a new member of the histone modification reader.
