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Author(s): Sefer Baday
In human cells, membrane proteins of the rhesus (Rh) family excrete ammonium and play a role in pH regulation. Based on high-resolution structures, Rh proteins are generally understood to act as NH3 channels. Given that cell membranes are permeable to gases...
Article GUID: 26190573
| Title: | Mechanism of NH4(+) Recruitment and NH3 Transport in Rh Proteins |
| Authors: | Sefer Baday |
| Link: | https://pubmed.ncbi.nlm.nih.gov/26190573/ |
| DOI: | 10.1016/j.str.2015.06.010 |
| Category: | |
| PMID: | 26190573 |
| Dept Affiliation: | CERMM
1 SIB Swiss Institute of Bioinformatics, Klingelbergstrasse 50/70, 4056 Basel, Switzerland; Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland. 2 Department of Chemistry and Biochemistry, Centre for Research in Molecular Modeling (CERMM), Concordia University, 7141 Sherbrooke Street West, Montréal, QC H4B 1R6, Canada. 3 Department of Chemistry and Biochemistry, Centre for Research in Molecular Modeling (CERMM), Concordia University, 7141 Sherbrooke Street West, Montréal, QC H4B 1R6, Canada. Electronic address: guillaume.lamoureux@concordia.ca. 4 SIB Swiss Institute of Bioinformatics, Klingelbergstrasse 50/70, 4056 Basel, Switzerland; Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland. Electronic address: simon.berneche@isb-sib.ch. |
Description: |
In human cells, membrane proteins of the rhesus (Rh) family excrete ammonium and play a role in pH regulation. Based on high-resolution structures, Rh proteins are generally understood to act as NH3 channels. Given that cell membranes are permeable to gases like NH3, the role of such proteins remains a paradox. Using molecular and quantum mechanical calculations, we show that a crystallographically identified site in the RhCG pore actually recruits NH4(+), which is found in higher concentration... |
