|PROSITE documentation PDOC51805 [for PROSITE entry PS51805]|
The extended plant homeodomain (ePHD) domain contains an N-terminal pre-PHD (C2HC zinc finger), a long linker, and a noncanonical PHD finger (C4HC3 zinc finger) (see <PDOC50016>). The ePHD domain can bind dsDNA but not histones [1,2,3,4].
The pre-PHD-type C2HC zinc finger and the PHD finger in the ePHD domain are associated with each other via extensive hydrophobic interactions and numerous hydrogen bonding interactions and folded as an intact structural module. The pre-PHD-type C2HC zinc finger consists of two α-helices separated by an anti-parallel β-sheet. Three cysteine residues and one histidine residue from the N-terminal loop, β2-strand, and α2-helix coordinate one zinc ion (designated Zn1). The C-terminal part of the ePHD domain is a PHD finger, consisting of one short anti-parallel β-sheet and one long anti-parallel β-sheet that are linked by one α helix (see <PDB:4NN2>). Like other PHD fingers, the PHD finger of the ePHD domain consists of two interleaved zinc fingers. A pair of bound zinc ions (designated Zn2 and Zn3) specifically stabilizes the characteristic cross-braced folding topology of the PHD finger. Each zinc ion is coordinated by a combination of four cysteine and histidine residues in which the Zn3 ion is coordinated by a C3H motif instead of a C4 motif [1,2].
Some proteins known to contain a ePHD domain are listed below:
The profile we developed covers both the pre-PHD-type C2HC zinc finger and the PHD finger of the ePHD domain.Last update:
June 2016 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Liu L. Qin S. Zhang J. Ji P. Shi Y. Wu J.|
|Title||Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA.|
|Source||J. Struct. Biol. 180:165-173(2012).|
|2||Authors||Liu Z. Li F. Ruan K. Zhang J. Mei Y. Wu J. Shi Y.|
|Title||Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6.|
|Source||J. Biol. Chem. 289:10069-10083(2014).|
|3||Authors||Chen S. Yang Z. Wilkinson A.W. Deshpande A.J. Sidoli S. Krajewski K. Strahl B.D. Garcia B.A. Armstrong S.A. Patel D.J. Gozani O.|
|Title||The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79.|
|Source||Mol. Cell 60:319-327(2015).|
|4||Authors||Klein B.J. Muthurajan U.M. Lalonde M.-E. Gibson M.D. Andrews F.H. Hepler M. Machida S. Yan K. Kurumizaka H. Poirier M.G. Cote J. Luger K. Kutateladze T.G.|
|Title||Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.|
|Source||Nucleic Acids Res. 44:472-484(2016).|