Ligand-Induced Variations in Structural and Dynamical Properties Within an Enzyme Superfamily.

ABSTRACT: Enzyme catalysis is a complex process involving several steps along the reaction coordinates, including substrate recognition and binding, chemical transformation, and product release. Evidence continues to emerge linking the functional and evolutionary role of conformational exchange processes in optimal catalytic activity. Ligand binding changes the conformational landscape of enzymes, inducing long-range conformational rearrangements. Using functionally distinct members of the pancreatic ribonuclease superfamily as a model system, we characterized the structural and conformational changes associated with the binding of two mononucleotide ligands. By combining NMR chemical shift titration experiments with the chemical shift projection analysis (CHESPA) and relaxation dispersion experimen

SUBMITTER: Narayanan C 

PROVIDER: S-EPMC6005897 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature