Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3P8D

Crystal structure of the second Tudor domain of human PHF20 (homodimer form)

Summary for 3P8D
Entry DOI10.2210/pdb3p8d/pdb
DescriptorMedulloblastoma antigen MU-MB-50.72 (2 entities in total)
Functional Keywordstudor domain, lysine-methylated p53 binding, histone binding, protein binding
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight15179.16
Authors
Cui, G.,Lee, J.,Thompson, J.R.,Botuyan, M.V.,Mer, G. (deposition date: 2010-10-13, release date: 2011-06-22, Last modification date: 2024-10-16)
Primary citationCui, G.,Park, S.,Badeaux, A.I.,Kim, D.,Lee, J.,Thompson, J.R.,Yan, F.,Kaneko, S.,Yuan, Z.,Botuyan, M.V.,Bedford, M.T.,Cheng, J.Q.,Mer, G.
PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53.
Nat.Struct.Mol.Biol., 19:916-924, 2012
Cited by
PubMed Abstract: PHF20 is a multidomain protein and subunit of a lysine acetyltransferase complex that acetylates histone H4 and p53 but whose function is unclear. Using biochemical, biophysical and cellular approaches, we determined that PHF20 is a direct regulator of p53. A Tudor domain in PHF20 recognized p53 dimethylated at Lys370 or Lys382 and a homodimeric form of this Tudor domain could associate with the two dimethylated sites on p53 with enhanced affinity, indicating a multivalent interaction. Association with PHF20 promotes stabilization and activation of p53 by diminishing Mdm2-mediated p53 ubiquitylation and degradation. PHF20 contributes to upregulation of p53 in response to DNA damage, and ectopic expression of PHF20 in different cell lines leads to phenotypic changes that are hallmarks of p53 activation. Overall our work establishes that PHF20 functions as an effector of p53 methylation that stabilizes and activates p53.
PubMed: 22864287
DOI: 10.1038/nsmb.2353
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon