9VXW

Cryo-EM structure of hAQP11 in LMNG

Summary for 9VXW

• Entry DOI: 10.2210/pdb9vxw/pdb
• EMDB information: 65443
• Descriptor: Aquaporin-11,sfGFP, DECANE (2 entities in total)
• Functional Keywords: membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 1
• Total formula weight: 60153.33

Authors

Suzuki, S.,Nishikawa, K.,Kamegawa, A.,kozai, D.,Fujiyoshi, Y. (deposition date: 2025-07-20, release date: 2025-12-31, Last modification date: 2026-07-15)

Primary citation

Suzuki, S.,Kamegawa, A.,Kozai, D.,Nishikawa, K.,Irie, K.,Fujiyoshi, Y.
Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.
Sci Adv, 12:eaeb5769-eaeb5769, 2026

PubMed 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.

PubMed: 41616064
DOI: 10.1126/sciadv.aeb5769

Experimental method

ELECTRON MICROSCOPY (2.3 Å)