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. 2016 Sep 2;16:177. doi: 10.1186/s12862-016-0743-8

Table 2.

Residues included in the stress-related patterns participate in the binding of p53 with DDR proteins

p53 interaction with protein (PDBID)/pattern residues sp53 (hp53) LL (ML) EXXA (DXXE) LM (LM)
P300 (2MZD) L45 binds to nonpolar patches on the surface of Taz2 domain of p300 Salt bridges and hydrogen bonds between D48 and E51 and Taz2 domain of p300
RPA70 (2B3G) Electrostatic interactions of D48 and E51 with RPA70N
CBP (2 L14, 1JSP) Hydrophobic interactions of M44,L45 with the NCBD domain of CBP Hydrophobic interactions of L383 and M384 with the bromodomain of CBP
P62 (2RUK) Electrostatic interaction of D48 and E51 with the PH domain of p62
Tfb1 (2GS0) Electrostatic interaction of E51 with Tfb1
HMGB1 (2LY4) Hydrophobic interaction of M44,L45 with HMGB1
Sir2 (1MA3) Hydrogen bond of L383 with sir2
S100B (1DT7) Hydrophobic interaction of L383 with S100B

Some of the residues composing the stress-related patterns in TAD2 and RD participate in Spalax (s) p53 direct interface with DDR proteins. Specific interactions via these residues between DDR proteins and human (h) p53 are described for each protein. The data for each protein was obtained from manuscripts related to the resolved structures of the protein complex with p53 in humans (PDBID is mentioned in the table for each protein)