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Structure of the stapled p53 peptide bound to Mdm2


Structure of the stapled p53 peptide bound to Mdm2

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dc.contributor.author Baek, Sohee pl
dc.contributor.author Kutchukian, Peter S. pl
dc.contributor.author Verdine, Gregory L. pl
dc.contributor.author Huber, Robert pl
dc.contributor.author Holak, Tadeusz [SAP14007479] pl
dc.contributor.author Lee, Ki Won pl
dc.contributor.author Popowicz, Grzegorz M. pl
dc.date.accessioned 2015-09-10T10:11:30Z
dc.date.available 2015-09-10T10:11:30Z
dc.date.issued 2012 pl
dc.identifier.issn 0002-7863 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/15517
dc.language eng pl
dc.title Structure of the stapled p53 peptide bound to Mdm2 pl
dc.type JournalArticle pl
dc.description.physical 103-106 pl
dc.description.additional Na publikacji autor podpisany: Tad A. Holak pl
dc.abstract.en Mdm2 is a major negative regulator of the tumor suppressor p53 protein, a protein that plays a crucial role in maintaining genome integrity. Inactivation of p53 is the most prevalent defect in human cancers. Inhibitors of the Mdm2 − p53 interaction that restore the functional p53 constitute potential nongenotoxic anticancer agents with a novel mode of action. We present here a 2.0 Å resolution structure of the Mdm2 protein with a bound stapled p53 peptide. Such peptides, which are conformationally and proteolytically stabilized with all-hydrocarbon staples, are an emerging class of biologics that are capable of disrupting protein − protein interactions and thus have broad therapeutic potential. The structure represents the first crystal structure of an i , i + 7 stapled peptide bound to its target and reveals that rather than acting solely as a passive conformational brace, a staple can intimately interact with the surface of a protein and augment the binding interface. pl
dc.description.volume 134 pl
dc.description.number 1 pl
dc.description.points 40 pl
dc.identifier.doi 10.1021/ja2090367 pl
dc.identifier.eissn 1520-5126 pl
dc.title.journal Journal of the American Chemical Society pl
dc.language.container eng pl
dc.affiliation Wydział Chemii : Zakład Chemii Organicznej pl
dc.subtype Article pl
dc.rights.original bez licencji pl
.pointsMNiSW [2012 A]: 40

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