De novo design of stable proteins that efficaciously inhibit oncogenic G proteins.
Ontology highlight
ABSTRACT: Many protein therapeutics are competitive inhibitors that function by binding to endogenous proteins and preventing them from interacting with native partners. One effective strategy for engineering competitive inhibitors is to graft structural motifs from a native partner into a host protein. Here, we develop and experimentally test a computational protocol for embedding binding motifs in de novo designed proteins. The protocol uses an "inside-out" approach: Starting with a structural model of the binding motif docked against the target protein, the de novo protein is built by growing new structural elements off the termini of the binding motif. During backbone assembly, a score function favors backbones that introduce new tertiary contacts within the designed protein and do not introduce
SUBMITTER: Cummins MC
PROVIDER: S-EPMC10360382 | biostudies-literature | 2023 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA