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Structural basis for ASPP2 recognition by the tumor suppressor p73.

Canning P, von Delft F, Bullock AN - J. Mol. Biol. (2012)

Bottom Line: The loop in p73 is changed by a two-residue insertion that also induces repacking around the site of the p53 mutational hotspot R175.Importantly, the binding of ASPP2 is preserved by conformational changes in both the ankyrin repeat and SH3 domains.These results further highlight the structural variation that impacts p53 family interactions within the p53 interactome.

View Article: PubMed Central - PubMed

Affiliation: Structural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Oxford OX3 7DQ, UK.

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Structural comparison of p53 and p73. (a) Superposition of the p53 (PDB 2OCJ) and p73 structures in the absence of DNA colored by Cα RMSD. Residues where the RMSD is higher than the scale maximum are colored white. (b) Comparison of the electrostatic surface potentials of the two proteins as calculated using PyMOL and APBS.28 The H1 helix and R268 are labeled for orientation.
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f0015: Structural comparison of p53 and p73. (a) Superposition of the p53 (PDB 2OCJ) and p73 structures in the absence of DNA colored by Cα RMSD. Residues where the RMSD is higher than the scale maximum are colored white. (b) Comparison of the electrostatic surface potentials of the two proteins as calculated using PyMOL and APBS.28 The H1 helix and R268 are labeled for orientation.

Mentions: Superposition of the p53 and p73 domains reveals a high degree of structural similarity (Fig. 2a). The overall Cα root-mean-square deviation (RMSD) between the two structures is 1.7 Å over 191 atoms, consistent with their high sequence conservation (61% identity, Fig. 1b). However, local regions of structural deviation are apparent when the RMSD values are examined across the different secondary‐structure elements (Fig. 2a). As expected, the lowest RMSD values lie in the core β-sandwich, whereas more significant deviation occurs across the DNA binding surface. Both proteins show a strongly electropositive surface potential across the DNA contact surface but more variable charge in the L2 loop, which mediates protein–protein interactions (Fig. 2b).


Structural basis for ASPP2 recognition by the tumor suppressor p73.

Canning P, von Delft F, Bullock AN - J. Mol. Biol. (2012)

Structural comparison of p53 and p73. (a) Superposition of the p53 (PDB 2OCJ) and p73 structures in the absence of DNA colored by Cα RMSD. Residues where the RMSD is higher than the scale maximum are colored white. (b) Comparison of the electrostatic surface potentials of the two proteins as calculated using PyMOL and APBS.28 The H1 helix and R268 are labeled for orientation.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3472557&req=5

f0015: Structural comparison of p53 and p73. (a) Superposition of the p53 (PDB 2OCJ) and p73 structures in the absence of DNA colored by Cα RMSD. Residues where the RMSD is higher than the scale maximum are colored white. (b) Comparison of the electrostatic surface potentials of the two proteins as calculated using PyMOL and APBS.28 The H1 helix and R268 are labeled for orientation.
Mentions: Superposition of the p53 and p73 domains reveals a high degree of structural similarity (Fig. 2a). The overall Cα root-mean-square deviation (RMSD) between the two structures is 1.7 Å over 191 atoms, consistent with their high sequence conservation (61% identity, Fig. 1b). However, local regions of structural deviation are apparent when the RMSD values are examined across the different secondary‐structure elements (Fig. 2a). As expected, the lowest RMSD values lie in the core β-sandwich, whereas more significant deviation occurs across the DNA binding surface. Both proteins show a strongly electropositive surface potential across the DNA contact surface but more variable charge in the L2 loop, which mediates protein–protein interactions (Fig. 2b).

Bottom Line: The loop in p73 is changed by a two-residue insertion that also induces repacking around the site of the p53 mutational hotspot R175.Importantly, the binding of ASPP2 is preserved by conformational changes in both the ankyrin repeat and SH3 domains.These results further highlight the structural variation that impacts p53 family interactions within the p53 interactome.

View Article: PubMed Central - PubMed

Affiliation: Structural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Oxford OX3 7DQ, UK.

Show MeSH
Related in: MedlinePlus