Flexibility-Induced Collective Behavior Drives Symmetry Breaking in Discrimination of Undesired Ions.

ABSTRACT: Structure flexibility is essential for the biological function of proteins. At the same time, many proteins need to discriminate ligands with subtle differences, with one example being ion selectivity. Investigating the mechanisms by which flexible proteins achieve such precise discrimination is crucial for advancing our understanding of their functions. In this work, we study transporter KCC4, which undergoes continuous conformation changes during ion transport and can realize K⁺ over Na⁺ selectivity. Our findings reveal that the center of the binding site no longer represents a stable equilibrium for the undesired Na⁺, and its binding mode exhibits bifurcation. Interestingly, protein conformation fluctuation can induce collective behavior throughout the e

SUBMITTER: Han B 

PROVIDER: S-EPMC11862943 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature