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  H95 is a pH-dependent gate in Aquaporin 4.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-32FE-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-3303-F
Genre: Journal Article

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 Creators:
Kaptan, S.1, Author              
Assentoft, M., Author
Schneider, H. P., Author
Fenton, R. A., Author
Deitmer, J. W., Author
MacAulay, N., Author
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578573              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2015-11-122015-12-01
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2015.08.020
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Title: Structure
Source Genre: Journal
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Pages: - Volume / Issue: 23 (12) Sequence Number: - Start / End Page: 2309 - 2318 Identifier: -