A Thermodynamic Model for Multivalency in 14-3-3 Protein-Protein Interactions.

ABSTRACT: Protein-protein interactions (PPIs) are at the core of molecular control over cellular function. Multivalency in PPI formation, such as via proteins with multiple binding sites and different valencies, requires fundamental understanding to address correlated challenges in pathologies and drug development. Thermodynamic binding models are needed to provide frameworks for describing multivalent PPIs. We established a model based on ditopic host-guest systems featuring the effective molarity, a hallmark property of multivalency, as a prime parameter governing the intramolecular binding in divalent interactions. By way of illustration, we study the interaction of the bivalent 14-3-3 protein scaffold with both the nonavalent CFTR and the hexavalent LRRK2 proteins, determining the underlying the

SUBMITTER: Stevers LM 

PROVIDER: S-EPMC6213025 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature