Conformational selection of vasopressin upon V_1a receptor binding.

ABSTRACT: The neuropeptide vasopressin (VP) and its three G protein-coupled receptors (V_1aR, V_1bR and V₂R) are of high interest in a wide array of drug discovery programs. V_1aR is of particular importance due to its cardiovascular functions and diverse roles in the central nervous system. The structure-activity relationships underpinning ligand-receptor interactions remain however largely unclear, hindering rational drug design. This is not least due to the high structural flexibility of VP in its free as well as receptor-bound states. In this work, we developed a novel approach to reveal features of conformational selectivity upon VP-V_1aR complex formation. We employed virtual screening strategies to probe VP's conformational space for transien

SUBMITTER: Che K 

PROVIDER: S-EPMC8567363 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature