Cryo-EM structure of the human Mas receptor reveals N-terminal occlusion of the orthosteric ligand binding pocket
as a structural element that occludes a conserved sub-pocket present in Mrgpr paralogs. Molecular docking simulation of the MasR agonist AR234960 provides a structural template for orthosteric ligand design. Together, these findings establish the structural framework for MasR.
Authors
- Yoshinori Fujiyoshi (ORCID: https://orcid.org/0000-0002-8070-1493)
- Kotaro Tanaka (ORCID: https://orcid.org/0000-0002-4205-0589)
- Kouki Nishikawa
- Shota Suzuki (ORCID: https://orcid.org/0000-0002-6516-8424)
Institutions
- The University of Tokyo (JP)
- Tokyo University of Agriculture and Technology (JP)
Publication Details
- Journal
- Journal of Molecular Biology
- Published
- 2026-05-01
- DOI
- https://doi.org/10.1016/j.jmb.2026.169844
- Primary Topic
- Receptor Mechanisms and Signaling
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Japan Society for the Promotion of Science