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2E61

Solution structure of the zf-CW domain in zinc finger CW-type PWWP domain protein 1

Summary for 2E61
Entry DOI10.2210/pdb2e61/pdb
NMR InformationBMRB: 11358,11359,11360,11361,11362
DescriptorZinc finger CW-type PWWP domain protein 1, ZINC ION (2 entities in total)
Functional Keywordszf-cw domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, unknown function
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight7713.76
Authors
He, F.,Muto, Y.,Inoue, M.,Kigawa, T.,Shirouzu, M.,Terada, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-12-25, release date: 2007-06-26, Last modification date: 2024-05-01)
Primary citationHe, F.,Umehara, T.,Saito, K.,Harada, T.,Watanabe, S.,Yabuki, T.,Kigawa, T.,Takahashi, M.,Kuwasako, K.,Tsuda, K.,Matsuda, T.,Aoki, M.,Seki, E.,Kobayashi, N.,Guntert, P.,Yokoyama, S.,Muto, Y.
Structural insight into the zinc finger CW domain as a histone modification reader
Structure, 18:1127-1139, 2010
Cited by
PubMed 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.
PubMed: 20826339
DOI: 10.1016/j.str.2010.06.012
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-10-30公开中

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