Structure-based inhibition of protein-protein interactions.

ABSTRACT: Protein-protein interactions (PPIs) are emerging as attractive targets for drug design because of their central role in directing normal and aberrant cellular functions. These interactions were once considered "undruggable" because their large and dynamic interfaces make small molecule inhibitor design challenging. However, landmark advances in computational analysis, fragment screening and molecular design have enabled development of a host of promising strategies to address the fundamental molecular recognition challenge. An attractive approach for targeting PPIs involves mimicry of protein domains that are critical for complex formation. This approach recognizes that protein subdomains or protein secondary structures are often present at interfaces and serve as organized scaffolds for t

SUBMITTER: Watkins AM 

PROVIDER: S-EPMC4362920 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature