Title of article :
Solution Structure of ASPP2 N-terminal Domain (N-ASPP2) Reveals a Ubiquitin-like Fold
Author/Authors :
Henning Tidow، نويسنده , , Antonina Andreeva، نويسنده , , Trevor J. Rutherford، نويسنده , , Alan R. Fersht، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
11
From page :
948
To page :
958
Abstract :
Proteins of the ASPP family bind to p53 and regulate p53-mediated apoptosis. Two family members, ASPP1 and ASPP2, have pro-apoptotic functions while iASPP shows anti-apoptotic responses. However, both the mechanism of enhancement/repression of apoptosis and the molecular basis for their different responses remain unknown. To address the role of the N-termini of pro-apoptotic ASPP proteins, we solved the solution structure of N-ASPP2 (1–83) by NMR spectroscopy. The structure of this domain reveals a β-Grasp ubiquitin-like fold. Our findings suggest a possible role for the N-termini of ASPP proteins in binding to other proteins in the apoptotic response network and thus mediating their selective pro-apoptotic function.
Keywords :
ASPP2 , NMR , ubiquitin-like , ?-Grasp , solution structure
Journal title :
Journal of Molecular Biology
Serial Year :
2007
Journal title :
Journal of Molecular Biology
Record number :
1249636
Link To Document :
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