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Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins
Author(s) -
Adams-Cioaba Melanie A.,
Li Zhihong,
Tempel Wolfram,
Guo Yahong,
Bian Chuanbing,
Li Yanjun,
Lam Robert,
Min Jinrong
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.02.012
Subject(s) - zinc finger , histone , transcription factor , biology , c terminus , domain (mathematical analysis) , transcription (linguistics) , microbiology and biotechnology , genetics , chemistry , amino acid , gene , mathematical analysis , linguistics , philosophy , mathematics
The human PHD finger protein 20 (PHF20) is a putative transcription factor. While little is known about its cognate cellular role, antibodies against PHF20 are present in sera from patients with hepatocellular carcinoma, glioblastoma and childhood medulloblastula. PHF20 comprises two N‐terminal Tudor domains, a central C2H2‐link zinc finger domain and a C‐terminal zinc‐binding PHD domain, and is a component of some MLL methyltransferase complexes. Here, we report the crystal structures of the N‐terminal Tudor domains of PHF20 and highlight the novel structural features of each domain. We also confirm previous studies suggesting that the second Tudor domain of PHF20 exhibits preference for dimethylated histone substrates.