Jagiellonian University Repository

Structure of the stapled p53 peptide bound to Mdm2

pcg.skipToMenu

Structure of the stapled p53 peptide bound to Mdm2

Show full item record

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


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)