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• W2991244815 startingPage "e0225784" @default.
• W2991244815 abstract "Our primary goal is to therapeutically target the oncogenic transcription factor MYC to stop tumor growth and cancer progression. Here, we report aspects of the biophysical states of the MYC protein and its interaction with one of the best-characterized MYC cofactors, TRansactivation/tRansformation-domain Associated Protein (TRRAP). The MYC:TRRAP interaction is critical for MYC function in promoting cancer. The interaction between MYC and TRRAP occurs at a precise region in the MYC protein, called MYC Homology Box 2 (MB2), which is central to the MYC transactivation domain (TAD). Although the MYC TAD is inherently disordered, this report suggests that MB2 may acquire a defined structure when complexed with TRRAP which could be exploited for the investigation of inhibitors of MYC function by preventing this protein-protein interaction (PPI). The MYC TAD, and in particular the MB2 motif, is unique and invariant in evolution, suggesting that MB2 is an ideal site for inhibiting MYC function." @default.
• W2991244815 created "2019-12-05" @default.
• W2991244815 creator A5044789565 @default.
• W2991244815 creator A5049815446 @default.
• W2991244815 creator A5049980044 @default.
• W2991244815 date "2019-12-02" @default.
• W2991244815 modified "2023-10-12" @default.
• W2991244815 title "Formation of a structurally-stable conformation by the intrinsically disordered MYC:TRRAP complex" @default.
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• W2991244815 doi "https://doi.org/10.1371/journal.pone.0225784" @default.
• W2991244815 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6886782" @default.
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• W2991244815 hasPublicationYear "2019" @default.
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