Journal
FEBS LETTERS
Volume 586, Issue 6, Pages 859-865Publisher
WILEY
DOI: 10.1016/j.febslet.2012.02.012
Keywords
PHD finger protein 20 (PHF20); Tudor domain; Royal Family; Crystal structure; Methyllysine; Histone binding
Funding
- Structural Genomics Consortium [1097737]
- Canadian Institutes for Health Research (CIHR)
- Canadian Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute
- GlaxoSmithKline
- Karolinska Institute
- Knut and Alice Wallenberg Foundation
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Merck Co., Inc.
- Novartis Research Foundation
- Swedish Agency for Innovation Systems
- Swedish Foundation for Strategic Research
- Wellcome Trust
- Natural Sciences and Engineering Research Council of Canada
- National Research Council Canada
- Province of Saskatchewan
- Western Economic Diversification Canada
- University of Saskatchewan
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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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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