Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.

ABSTRACT: Among the long-standing efforts to elucidate the physical mechanisms of protein-ligand catch bonding, particular attention has been directed at the family of selectin proteins. Selectins exhibit slip, catch-slip, and slip-catch-slip bonding, with minor structural modifications causing major changes in selectins' response to force. How can a single structural mechanism allow interconversion between these various behaviors? We present a unifying theory of selectin-ligand catch bonding, using a structurally motivated free energy landscape to show how the topology of force-induced deformations of the molecular system produces the full range of observed behaviors. We find that the pathway of bond rupture deforms in non-trivial ways, such that unbinding dynamics depend sensitively on force. This

SUBMITTER: Barkan CO 

PROVIDER: S-EPMC10861892 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature