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TitleCryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.
Journal, issue, pagesSci Adv, Vol. 12, Issue 5, Page eaeb5769, Year 2026
Publish dateJan 30, 2026
AuthorsShota Suzuki / Akiko Kamegawa / Daisuke Kozai / Kouki Nishikawa / Katsumasa Irie / Yoshinori Fujiyoshi /
PubMed AbstractAquaporin-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 ...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.
External linksSci Adv / PubMed:41616064 / PubMed Central
MethodsEM (single particle)
Resolution2.3 Å
Structure data

65443

9vxw

EMDB-65443, PDB-9vxw:
Cryo-EM structure of hAQP11 in LMNG
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

ChemComp-D10:
DECANE

Source
  • homo sapiens (human)
  • aequorea victoria (jellyfish)
KeywordsMEMBRANE PROTEIN

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