Biochemical and biophysical approaches to study the structure and function of the chloride channel (ClC) family of proteins.
Détails
ID Serval
serval:BIB_36CB2BB6B535
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Biochemical and biophysical approaches to study the structure and function of the chloride channel (ClC) family of proteins.
Périodique
Biochimie
ISSN
1638-6183 (Electronic)
ISSN-L
0300-9084
Statut éditorial
Publié
Date de publication
2016
Peer-reviewed
Oui
Volume
128-129
Pages
154-162
Langue
anglais
Notes
Publication types: Journal Article ; Review
Publication Status: ppublish
Publication Status: ppublish
Résumé
The chloride channel (ClC) protein family comprises both chloride (Cl(-)) channels and chloride/proton (Cl(-)/H(+)) antiporters. In prokaryotes and eukaryotes, these proteins mediate the movement of Cl(-) ions across the membrane. In eukaryotes, ClC proteins play a role in the stabilization of membrane potential, epithelial ion transport, hippocampal neuroprotection, cardiac pacemaker activity and vesicular acidification. Moreover, mutations in the genes encoding ClC proteins can cause genetic disease in humans. In prokaryotes, the Cl(-)/H(+) antiporters, such as ClC-ec1 found in Escherichia coli promote proton expulsion in the extreme acid-resistance response common to enteric bacteria. To date, structural and functional studies of the prokaryotic protein have revealed unique structural features, including complicated transmembrane topology with 18 α-helices in each subunit and an anion-coordinating region in each subunit. Several different approaches such as X-ray crystallography, NMR, biochemical studies, and molecular dynamics simulations have been applied to the study of ClC proteins. Continued study of the unique structure and function of this diverse family of proteins has the potential to lead to the development of novel therapeutic targets for neuronal, renal, bone, and food-borne diseases.
Mots-clé
Binding Sites, Biochemical Phenomena, Biophysical Phenomena, Chloride Channels/chemistry, Chloride Channels/metabolism, Crystallography, X-Ray, Escherichia coli Proteins/chemistry, Escherichia coli Proteins/metabolism, Humans, Molecular Dynamics Simulation, Protein Domains, Protein Structure, Secondary, Acid resistance, Antiporter, Channel, Chloride ion, Membrane protein, Proton
Pubmed
Web of science
Open Access
Oui
Création de la notice
09/06/2023 16:02
Dernière modification de la notice
20/07/2023 6:57