Ontology highlight
ABSTRACT:
SUBMITTER: Kritzer JA
PROVIDER: S-EPMC2873023 | biostudies-literature | 2005 Oct
REPOSITORIES: biostudies-literature
Kritzer Joshua A JA Luedtke Nathan W NW Harker Elizabeth A EA Schepartz Alanna A
Journal of the American Chemical Society 20051001 42
Recently we described a beta-decapeptide (beta53-1) that folds into a 14-helix in aqueous solution, binds the oncoprotein hDM2 with submicromolar affinity, and inhibits the interaction of hDM2 with a peptide derived from the activation domain of p53 (p53AD). The solution structure of beta53-1 in CD3OH revealed an unexpected C-terminal unwinding that staggers the side chains comprising the hDM2 recognition epitope to better mimic those of p53AD. The structure-function relationship implied by this ...[more]