ASPP (apoptosis-stimulating protein of p53) 2 is a pro-apoptotic protein that stimulates the p53-mediated apoptotic response. Here, we provide an overview of the structure and protein–protein interactions of ASPP2. The C-terminus of ASPP2 contains Ank (ankyrin) repeats and an SH3 domain (Src homology 3 domain). The Ank–SH3 domains mediate interactions between ASPP2 and numerous proteins involved in apoptosis such as p53 and Bcl-2. The proline-rich domain of ASPP2 is unfolded in its native state, but was not shown to mediate intermolecular interactions. Instead, it makes an intramolecular domain–domain interaction with the Ank–SH3 C-terminal domains of ASPP2. This intramolecular interaction between the unstructured proline-rich domain and the structured Ank–SH3 domains in ASPP2, which is possible due to the unfolded nature of the proline-rich domain, is proposed to have an important role in regulating the intermolecular interactions of ASPP2 with its partner proteins.
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November 2007
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Conference Article|
October 25 2007
Insights into the structure and protein–protein interactions of the pro-apoptotic protein ASPP2
S. Rotem;
S. Rotem
1Department of Organic Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel
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C. Katz;
C. Katz
1Department of Organic Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel
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A. Friedler
A. Friedler
1
1Department of Organic Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel
1To whom correspondence should be addressed (email assaf@chem.ch.huji.ac.il).
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Biochem Soc Trans (2007) 35 (5): 966–969.
Article history
Received:
June 11 2007
Citation
S. Rotem, C. Katz, A. Friedler; Insights into the structure and protein–protein interactions of the pro-apoptotic protein ASPP2. Biochem Soc Trans 1 November 2007; 35 (5): 966–969. doi: https://doi.org/10.1042/BST0350966
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