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The MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-XL-binding motif.

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The MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-XL-binding motif.

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dc.contributor.author Xu, Huibin.
dc.contributor.author Ye, Hong.
dc.contributor.author Osman, Nur Eliza.
dc.contributor.author Sadler, Kristen.
dc.contributor.author Won, Eun-Young.
dc.contributor.author Chi, Seung-Wook.
dc.contributor.author Yoon, Ho Sup.
dc.date.accessioned 2012-01-26T01:28:28Z
dc.date.available 2012-01-26T01:28:28Z
dc.date.copyright 2009
dc.date.issued 2012-01-26
dc.identifier.citation Xu, H., Ye, H., Osman, N. E., Sadler, K., Won, E. -Y., Chi, S. -W., et al. (2009). The MDM2-Binding Region in the Transactivation Domain of p53 Also Acts as a Bcl-XL-Binding Motif, Biochemistry, 48(51), 12159-12168.
dc.identifier.uri http://hdl.handle.net/10220/7476
dc.description.abstract While the transcription-dependent mechanism of p53 has been extensively studied, recently the transcription-independent apoptotic activity of p53 has also been described. Bcl-2 and Bcl-XL interact with p53 and induce apoptosis. Initially, the p53 DNA-binding domain (p53DBD) was found to bind to Bcl-2 and Bcl-XL. Later, the p53 N-terminal domain (p53NTD) was reported to be sufficient for inducing the transcription-independent apoptotic activity of p53 and also shown to interact with Bcl-XL. Here, we further document that the transactivation domain of p53 (p53TAD) in p53NTD alone binds to Bcl-XL. We demonstrated that the MDM2-binding region (residues S15 to N29, herein referred to as SN15) in p53TAD is the binding site for Bcl-XL. The binding interface on Bcl-XL was identified at the hydrophobic pocket formed by the BH1, BH2, and BH3 domains, which also binds to the Bak/Bad BH3 peptides, suggesting Bcl-XL and MDM2 share a common binding motif in p53TAD. Our NMR structural studies have shown that the SN15 peptide undergoes a conformational change upon binding to Bcl-XL. A Bcl-XL/SN15 complex structural model suggests that the SN15 peptide adopts an extended α-helical structure to bind to the hydrophobic pocket on the Bcl-XL, which is similar to the mode of binding between BH3 peptides and Bcl-XL.
dc.language.iso en
dc.relation.ispartofseries Biochemistry
dc.rights © 2009 American Chemical Society.
dc.subject DRNTU::Science::Biological sciences::Biochemistry.
dc.title The MDM2-binding region in the transactivation domain of p53 also acts as a Bcl-XL-binding motif.
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1021/bi901188s

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