BcL-xL conformational changes upon fragment binding revealed by NMR.

ABSTRACT: Protein-protein interactions represent difficult but increasingly important targets for the design of therapeutic compounds able to interfere with biological processes. Recently, fragment-based strategies have been proposed as attractive approaches for the elaboration of protein-protein surface inhibitors from fragment-like molecules. One major challenge in targeting protein-protein interactions is related to the structural adaptation of the protein surface upon molecular recognition. Methods capable of identifying subtle conformational changes of proteins upon fragment binding are therefore required at the early steps of the drug design process. In this report we present a fast NMR method able to probe subtle conformational changes upon fragment binding. The approach relies on the compari

SUBMITTER: Aguirre C 

PROVIDER: S-EPMC3662666 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature