The anti-Mullerian hormone prodomain is displaced from the hormone/prodomain complex upon bivalent binding to the hormone receptor.

ABSTRACT: Noncovalent complexes of transforming growth factor-β family growth/differentiation factors with their prodomains are classified as latent or active, depending on whether the complexes can bind their respective receptors. For the anti-Müllerian hormone (AMH), the hormone-prodomain complex is active, and the prodomain is displaced upon binding to its type II receptor, AMH receptor type-2 (AMHR2), on the cell surface. However, the mechanism by which this displacement occurs is unclear. Here, we used ELISA assays to measure the dependence of prodomain displacement on AMH concentration and analyzed results with respect to the behavior expected for reversible binding in combination with ligand-induced receptor dimerization. We found that, in solution, the prodomain has a high affinity for the g

SUBMITTER: Cate RL 

PROVIDER: S-EPMC8801479 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature