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Structural Insight into the Zinc Finger CW Domain as a Histone Modification Reader
- Source :
-
Structure . Sep2010, Vol. 18 Issue 9, p1127-1139. 13p. - Publication Year :
- 2010
-
Abstract
- Summary: 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09692126
- Volume :
- 18
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Structure
- Publication Type :
- Academic Journal
- Accession number :
- 53406005
- Full Text :
- https://doi.org/10.1016/j.str.2010.06.012