3Q1J

Crystal structure of tudor domain 1 of human PHD finger protein 20

Summary for 3Q1J

• Entry DOI: 10.2210/pdb3q1j/pdb
• Descriptor: PHD finger protein 20, UNKNOWN ATOM OR ION (3 entities in total)
• Functional Keywords: tudor domain, mbt, structural genomics consortium, sgc, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q9BVI0
• Total number of polymer chains: 1
• Total formula weight: 8211.17

Authors

Tempel, W.,Li, Z.,Wernimont, A.K.,Chao, X.,Bian, C.,Lam, R.,Crombet, L.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2010-12-17, release date: 2011-02-09, Last modification date: 2023-09-13)

Primary citation

Adams-Cioaba, M.A.,Li, Z.,Tempel, W.,Guo, Y.,Bian, C.,Li, Y.,Lam, R.,Min, J.
Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins.
Febs Lett., 586:859-865, 2012

PubMed Abstract: 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.

PubMed: 22449972
DOI: 10.1016/j.febslet.2012.02.012

Experimental method

X-RAY DIFFRACTION (2.35 Å)