IndraLab
Statements
sparser
"In a previous study, we determined the structure of the complex between the p53-TAD2 peptide (residues 41–62), doubly phosphorylated on Ser46 and Thr55, and p62-PH of TFIIH using NMR and revealed that phosphorylated Ser46 and Thr55 make electrostatic contacts with K18/K19 and K54, respectively, of p62-PH ( xref ). xref (Note that, to avoid confusion, residues of p53 and XPC are represented by three-letter code and those of p62 are represented by one-letter code in this paper.) We also quantitatively examined the effects of phosphorylation of p53-TAD2 on binding to p62-PH by using isothermal titration calorimetry (ITC) and NMR."
sparser
"In contrast, phosphorylation of Ser46 at the p53 TAD2 domain by c-Jun NH2-terminal kinase 2α2 (JNK2α2) exerts a weaker influence on the binding affinity, whereas phosphorylation of Ser376 and Ser378 at the C-terminus of p53 by protein kinase C (PKC) appears to have little effect."
sparser
"To demonstrate this, here we focused on phosphorylated p53-TAD2 and its interaction with one of its targets, p62-PH of the general transcription factor TFIIH, because of the availability of the structure of this complex. xref Knowledge of tertiary structure can help us to correctly interpret experimental results."