ArticleProceedings of the National Academy of Sciences of the United States of America2021
Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- The best ovarian reserve marker to predict ovarian response following controlled ovarian hyperstimulation: a systematic review and meta-analysis.Systematic reviews · 2024Pooled it
- Novel anti-Mullerian hormone receptor 2 binding peptide prevents chemotherapy-related ovarian follicle loss in a mouse model.Journal of assisted reproduction and genetics · 2026Article
- The role of anti-Müllerian hormone as a therapeutic agent to preserve the ovarian follicle pool during chemotherapy.Journal of assisted reproduction and genetics · 2026Review
- Molecular mechanisms and multi-organ regulatory roles of anti-Müllerian hormone in female reproduction.Communications biology · 2026Review
- Genetic and functional characterization of AMH Signaling in Zebrafish - Evidence for Roles of Amh-Bmpr2a-Bmpr1bb Pathway in Controlling Gonadal Homeostasis.PLoS genetics · 2026Article
- Epigenetic regulation by DNA methylation in PCOS and POI: mechanisms of ovarian dysfunction and implications for clinical research.Journal of ovarian research · 2026Review
- Amhy/Amhr2y-mediated sex determination in two distantly related teleosts relies on the conserved Alk3-Smad5 axis.Molecular biology and evolution · 2026Article
- Endoglin as a BMP9 co-receptor in vascular endothelial cells: prodomain displacement and TGFBRII recruitment.Nature communications · 2025Article
- Anti-Müllerian hormone plays a bidirectional role in cancer: a multi-database and multi-method study.Discover oncology · 2025Article
- Role of cellular prion protein in mouse granulosa cells and its effects on ovarian function in knockout mice.Molecular medicine reports · 2025Article
- Anti-Müllerian hormone binds heat shock protein glucose-regulated protein 78 in human follicular fluid.Journal of assisted reproduction and genetics · 2025Article
- PepTune:ArXiv · 2025Article
- AMHY and sex determination in egg-laying mammals.Genome biology · 2025Article
- Anti-Müllerian hormone in PCOS: Molecular regulation and emerging therapeutic strategies.Biomolecules & biomedicine · 2025Review
- Gene therapy with feline anti-Müllerian hormone analogs disrupts folliculogenesis and induces pregnancy loss in female domestic cats.Nature communications · 2025Article
- Dose-dependent role of AMH and AMHR2 signaling in male differentiation and regulation of sex determination in Spotted knifejaw (Oplegnathus punctatus) with XCell communication and signaling : CCS · 2025Article
- A divergent two-domain structure of the anti-Müllerian hormone prodomain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Regulation of Curcumin on Follicle Initiation Rate in Diminished Ovarian Reserve.Combinatorial chemistry & high throughput screening · 2025Article
- Article
- Multi-genome comparisons reveal gain-and-loss evolution of anti-Mullerian hormone receptor type 2 as a candidate master sex-determining gene in Percidae.BMC biology · 2024Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Anti-Müllerian hormone (AMH), or Müllerian-inhibiting substance, is a protein hormone that promotes Müllerian duct regression during male fetal sexual differentiation and regulation of folliculogenesis in women. AMH is a member of the transforming growth factor beta (TGF-β) family, which has evolved to signal through its own dedicated type II receptor, AMH receptor type II (AMHR2). Structures of other TGF-β family members have revealed how ligands infer specificity for their cognate receptors; however, it is unknown how AMH binds AMHR2 at the molecular level. Therefore, in this study, we solved the X-ray crystal structure of AMH bound to the extracellular domain of AMHR2 to a resolution of 2.6Å. The structure reveals that while AMH binds AMHR2 in a similar location to Activin and BMP ligand binding to their type II receptors, differences in both AMH and AMHR2 account for a highly specific interaction. Furthermore, using an AMH responsive cell-based luciferase assay, we show that a conformation in finger 1 of AMHR2 and a salt bridge formed by K534 on AMH and D81/E84 of AMHR2 are key to the AMH/AMHR2 interaction. Overall, our study highlights how AMH engages AMHR2 using a modified paradigm of receptor binding facilitated by modifications to the three-finger toxin fold of AMHR2. Furthermore, understanding these elements contributing to the specificity of binding will help in the design of agonists or antagonists or the selection of antibody therapies.
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