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PMID: 18768791 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

High-resolution x-ray structure of human aquaporin 5.

Horsefield R, Nordén K, Fellert M, Backmark A, Törnroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R

Abstract

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-A 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.

MeSH Terms
Aquaporin 5/chemistry Crystallization Crystallography, X-Ray Humans Lipids/chemistry Models, Molecular Protein Structure, Quaternary Protein Structure, Tertiary Structural Homology, Protein
Chemicals
Aquaporin 5 Lipids
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Horsefield Rob
Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, SE-405 30 Göteborg, Sweden.
Nordén Kristina
Fellert Maria
Backmark Anna
Törnroth-Horsefield Susanna
Terwisscha van Scheltinga Anke C
Kvassman Jan
Kjellbom Per
Johanson Urban
Neutze Richard
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
1091-6490
Published
2008-09-09
Epub
2008-00-03
Pages
13327-32
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC2533189
Subset
IM
Databases
PDB
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