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Rescuing p53 from mdm2 by intrinsically unfolded SUMO protease 4
Do-Hyoung Kim1, Chewook Lee1, Bom Kim1, Si-Hyung Lee1, Kyou-Hoon Han1,*
1Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Korea
Many intrinsically unstructured/unfolded proteins (IUPs) contain transient local secondary structures even though they are “unstructured” in a tertiary sense. These local secondary structures are named “pre-structured motifs (PreSMos)” and in fact are the specificity determinants for IUP-target binding, i.e., the active sites in IUPs. Using high-resolution NMR we have delineated a PreSMo active site in the intrinsically unfolded mid-domain (residues 201-300) of SUMO-specific protease 4 (SUSP4). This 29-residue motif which we termed a p53 rescue motif can protect p53 from mdm2 quenching by binding to the p53-helix binding pocket in mdm2(3-109). Our work demonstrates that the PreSMo approach is quite effective in providing a structural rationale for interactions of p53-mdm2-SUSP4 and opens a novel avenue for designing mdm2-inhibiting anticancer compounds.
Abstract, Accepted Manuscript(in press) [Submitted on July 14, 2017, Accepted on July 14, 2017]
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