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- W2010438894 abstract "Vasopressin and oxytocin are intrinsically disordered cyclic nanopeptides belonging to a family of neurohypophysial hormones. Vasopressin is an antidiuretic, regulating the retention of water and salts in mammals by indirectly promoting the insertion of aquaporin-2 channels into the epithelial cells of kidney nephron collecting ducts. Oxytocin, in contrast, is a neurotransmitter responsible for inducing labor and the subsequent lactation, as well as modulating some social behaviors. Although unique in their functions, these peptides only differ by two residues and both feature a tocin ring formed by the disulfide bridge between 1st and 6th cysteine residues. This structural similarity was experimentally linked to inhibition of activity at vasopressin receptors by the present oxytocin. Conversely, previous studies have also shown that single-residue mutations in both peptides have a significant impact on their receptor specificities.In this study we perform molecular dynamics (MD) simulations of wild type and mutant oxytocin and vasopressin in order to characterize their structural ensembles and relate them to the observed variation in activity. The generated ensembles of Y21H and P26L mutants of vasopressin and Q23T and Q23T,P26G mutants of oxytocin reveal significant population shifts compared to the wild type peptides. Here we present the classification of these populations based on the distribution of radius of gyration and deformation of the tocin ring, and attempt to relate the structural changes to the experimentally determined peptide activity and carrier protein binding affinity." @default.
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- W2010438894 date "2014-01-01" @default.
- W2010438894 modified "2023-09-26" @default.
- W2010438894 title "Computational Characterization of the Disordered Ensembles of Vasopressin and Oxytocin" @default.
- W2010438894 doi "https://doi.org/10.1016/j.bpj.2013.11.2719" @default.
- W2010438894 hasPublicationYear "2014" @default.
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