Keyword search (4,164 papers available)

"Sefer Baday" Authored Publications:

Title Authors PubMed ID
1 Mechanism of NH4(+) Recruitment and NH3 Transport in Rh Proteins Sefer Baday 26190573
CERMM

 

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
Publication:Structure (London, England : 1993)
Keywords:
PMID:26190573 Category: Date Added:2015-07-21
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...




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