Wrapping effects within a proposed function-rescue strategy for the Y220C oncogenic mutation of protein p53.

ABSTRACT: Soluble proteins must protect their structural integrity from water attack by wrapping interactions which imply the clustering of nonpolar residues around the backbone hydrogen bonds. Thus, poorly wrapped hydrogen bonds constitute defects which have been identified as promoters of protein associations since they favor the removal of hydrating molecules. More specifically, a recent study of our group has shown that wrapping interactions allow the successful identification of protein binding hot spots. Additionally, we have also shown that drugs disruptive of protein-protein interfaces tend to mimic the wrapping behavior of the protein they replace. Within this context, in this work we study wrapping three body interactions related to the oncogenic Y220C mutation of the tumor suppressor prot

SUBMITTER: Accordino SR 

PROVIDER: S-EPMC3554699 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature