Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein.

ABSTRACT: In cellular environments, proteins not only interact with their specific partners but also encounter a high concentration of bystander macromolecules, or crowders. Nonspecific interactions with macromolecular crowders modulate the activities of proteins, but our knowledge about the rules of nonspecific interactions is still very limited. In previous work, we presented experimental evidence that macromolecular crowders acted competitively in inhibiting the binding of maltose binding protein (MBP) with its ligand maltose. Competition between a ligand and an inhibitor may result from binding to either the same site or different conformations of the protein. Maltose binds to the cleft between two lobes of MBP, and in a series of mutants, the affinities increased with an increase in the extent

SUBMITTER: Ghosh A 

PROVIDER: S-EPMC6703856 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature