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Zeitschriftenartikel

H95 is a pH-dependent gate in Aquaporin 4.

MPG-Autoren
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Kaptan,  S.
Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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de Groot,  B. L.
Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

Volltexte (frei zugänglich)

2239081.pdf
(Verlagsversion), 3MB

Ergänzendes Material (frei zugänglich)

2239081_Suppl_1.pdf
(Ergänzendes Material), 688KB

2239081_Suppl_2.pdf
(Ergänzendes Material), 4MB

Zitation

Kaptan, S., Assentoft, M., Schneider, H. P., Fenton, R. A., Deitmer, J. W., MacAulay, N., et al. (2015). H95 is a pH-dependent gate in Aquaporin 4. Structure, 23(12), 2309-2318. doi:10.1016/j.str.2015.08.020.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0029-32FE-5
Zusammenfassung
Aquaporin 4 (AQP4) is a transmembrane protein from the aquaporin family and is the predominant water channel in the mammalian brain. The regulation of permeability of this protein could be of potential therapeutic use to treat various forms of damage to the nervous tissue. In this work, based on data obtained from insilico and invitro studies, a pH sensitivity that regulates the osmotic water permeability of AQP4 is demonstrated. The results indicate that AQP4 has increased water permeability at conditions of low pH in atomistic computer simulations and experiments carried out on Xenopus oocytes expressing AQP4. With molecular dynamics simulations, this effect was traced to a histidine residue (H95) located in the cytoplasmic lumen of AQP4. A mutant form of AQP4, in which H95 was replaced with an alanine (H95A), loses sensitivity to cytoplasmic pH changes in invitro osmotic water permeability, thereby substantiating the insilico work.