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High-resolution x-ray structure of human aquaporin 5

  • Rob Horsefield
  • Kristina Nordén
  • Maria Agemark
  • Anna Backmark
  • Susanna Tornroth-Horsefield
  • Anke C. Terwisscha van Scheltinga
  • Jan Kvassman
  • Per Kjellbom
  • Urban Johanson
  • Richard Neutze
Publiceringsår: 2008
Språk: Engelska
Sidor: 13327-13332
Publikation/Tidskrift/Serie: Proceedings of the National Academy of Sciences
Volym: 105
Nummer: 36
Dokumenttyp: Artikel i tidskrift
Förlag: National Acad Sciences


Human aquaporin 5 (HsAQP5)facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-angstrom resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking.


  • Biological Sciences
  • heterologous overexpression
  • crystallography
  • water channel protein
  • trafficking
  • membrane protein


  • ISSN: 1091-6490

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