Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore
Abstract
Aquaporin-11 (AQP-11) is an endoplasmic reticulum-localized water channel essential for renal development. Its structure and the molecular basis of its transport properties remained unknown. We analyzed the human AQP11 structure under cryo-electron microscopy at 2.3 Å resolution, revealing a trimeric architecture compared with other known tetrameric AQPs and a topology comprising seven transmembrane helices (Hs), including an additional N-terminal helix (H0). The channel pore is broader and more hydrophobic than that of canonical AQPs, and features a unique structure surrounding an Asn-Pro-Cys (NPC) sequence instead of the typical Asn-Pro-Ala (NPA) motif. These features provide a structural framework through which water and other small solutes can permeate AQP11. Our findings provide a blueprint for designing specific inhibitors to investigate the physiologic functions of AQP11.
Fields of Study & Subjects
Ion Transport and Channel Regulation
ATP Synthase and ATPases Research
Ion channel regulation and function
Publication details
- Journal / source
- Science Advances
- Publisher
- American Association for the Advancement of Science (AAAS)
- Volume
- 12
- Issue
- 5
- Pages
- eaeb5769–eaeb5769
- Publication date
- 30 January 2026
- Language
- EN