Clinical Genomics Unit, Tumor Biology Section, Head, Neck Surgery Branch, National Institute on Deafness, Other Communication Disorders, NIH, Bethesda, MD, 20892, USA
TP63 binds DNA as either a homo- or a heterotetramer, with isoform composition of the tetramer possibly determining transactivation activity. p63 may also form mixed dimers or tetramers with p73 at relatively higher affinity than with p53, suggesting functional cross talk to regulate transcriptional activity (Davison et al., 1999; Natan and Joerger, 2012). p63 appears to form a dimer of dimers, with monomers consisting of a β-strand followed by two helices (H1 and H2) that adopt a z-shaped double-hairpin conformation with little intramolecular contact between structural elements (Natan and Joerger, 2012). Monomers dimerize via intermolecular antiparallel β-sheet interactions and antiparallel packing of the H1 helices, with important hydrophobic contacts made by key leucine, valine, tyrosine, methionine, and isoleucine residues (Natan and Joerger, 2012). Tetramers are formed by hydrophobic H1-H1 interactions and H2-mediated contact where the H2 helices from the primary dimer clasps the adjacent dimer, packing the tetramer in an orthogonal fashion via H1 helices arrangement (Natan and Joerger, 2012). Analysis of the DBD of TP63 shows higher similarity to that of p73 than p53, and appears to bind a 10-bp DNA sequence containing a "CATG" motif with A/T-rich flanking regions (Chen et al., 2011).
Austin Mattox ; Zhong Chen ; Carter Van Waes
TP63 (tumor protein p63)
Atlas Genet Cytogenet Oncol Haematol. 2012-12-01
Online version: http://www.atlasgeneticsoncology.org/gene/365/tp63-(tumour-protein-p63)