ArticleThe Journal of physiology2003
Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore.
Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Two positively charged amino acid side-chains in the inner vestibule of the CFTR channel pore play analogous roles in controlling anion binding and anion conductance.Cellular and molecular life sciences : CMLS · 2021Article
- Architecture and functional properties of the CFTR channel pore.Cellular and molecular life sciences : CMLS · 2017Review
- The cystic fibrosis transmembrane conductance regulator is an extracellular chloride sensor.Pflugers Archiv : European journal of physiology · 2015Article
- Impact of the F508del mutation on ovine CFTR, a Cl- channel with enhanced conductance and ATP-dependent gating.The Journal of physiology · 2015Article
- Location of a permeant anion binding site in the cystic fibrosis transmembrane conductance regulator chloride channel pore.The journal of physiological sciences : JPS · 2015Article
- Article
- Pseudohalide anions reveal a novel extracellular site for potentiators to increase CFTR function.British journal of pharmacology · 2012Article
- Relative movements of transmembrane regions at the outer mouth of the cystic fibrosis transmembrane conductance regulator channel pore during channel gating.The Journal of biological chemistry · 2012Article
- Cystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Biochemistry · 2012Article
- Differential contribution of TM6 and TM12 to the pore of CFTR identified by three sulfonylurea-based blockers.Pflugers Archiv : European journal of physiology · 2012Article
- Divergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, glibenclamide, and GlyH-101.American journal of physiology. Cell physiology · 2012Article
- Molecular models of the open and closed states of the whole human CFTR protein.Cellular and molecular life sciences : CMLS · 2009Article
- Novel residues lining the CFTR chloride channel pore identified by functional modification of introduced cysteines.The Journal of membrane biology · 2009Article
- Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore.Pflugers Archiv : European journal of physiology · 2008Article
- Direct and indirect effects of mutations at the outer mouth of the cystic fibrosis transmembrane conductance regulator chloride channel pore.The Journal of membrane biology · 2007Article
- On the origin of asymmetric interactions between permeant anions and the cystic fibrosis transmembrane conductance regulator chloride channel pore.Biophysical journal · 2007Article
- Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel.The Journal of general physiology · 2006Article
- CFTR channel pharmacology: novel pore blockers identified by high-throughput screening.The Journal of general physiology · 2004Review
- Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore.The Journal of general physiology · 2003Article
- Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore.The Biochemical journal · 2003Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chloride permeation through the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel is blocked by highly lyotropic permeant anions which bind tightly within the pore. Here we show that several different substitutions of a positively charged amino acid residue, arginine R334, in the putative outer mouth of the CFTR pore, greatly reduce the block caused by lyotropic Au(CN)2- ions applied to the intracellular side of the channel. Fixed positive charge at this site appears to play a role in Au(CN)2- binding, as judged by multiple substitutions of differently charged amino acid side chains and also by the pH dependence of block conferred by the R334H mutant. However, non-charge-dependent effects also appear to contribute to Au(CN)2- binding. Mutation of R334 also disrupts the apparent electrostatic interaction between intracellular Au(CN)2- ions and extracellular permeant anions, an interaction which normally acts to relieve channel block. All six mutations studied at R334 significantly weakened this interaction, suggesting that arginine possesses a unique ability to coordinate ion-ion interactions at this site in the pore. Our results suggest that lyotropic anions bind tightly to a site in the outer mouth of the CFTR pore that involves interaction with a fixed positive charge. Binding to this site is also involved in coordination of multiple permeant anions within the pore, suggesting that anion binding in the outer mouth of the pore is an important aspect in the normal anion permeation mechanism.
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