From glutathione transferase to pore in a CLIC.
Many plasma membrane chloride channels have been cloned and characterized in great detail. In contrast, very little is known about intracellular chloride channels. Members of a novel class of such channels, called the CLICs (chloride intracellular channels), have been identified over the last few years. A striking feature of the CLIC family of ion channels is that they can exist in a water-soluble state as well as a membrane-bound state. A major step forward in understanding the functioning of these channels has been the recent crystal structure determination of one family member, CLIC1. The structure confirms that CLICs are members of the glutathione S-transferase superfamily and provides clues as to how CLICs can insert into membranes to form chloride channels.
Biota Structural Biology Laboratory, St. Vincent's Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065, Australia.
Brett A
BA
Cromer
Craig J
CJ
Morton
Philip G
PG
Board
Michael W
MW
Parker
D000595:Amino Acid Sequence; D018118:Chloride Channels / Q000737:chemistry* / Q000145:classification* / Q000235:genetics; D003461:Crystallography / Q000379:methods; D019143:Evolution, Molecular; D005982:Glutathione Transferase / Q000737:chemistry* / Q000145:classification; D007425:Intracellular Membranes / Q000502:physiology; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016062:Porosity; D017434:Protein Structure, Tertiary
D018118:Chloride Channels; D005982:Glutathione Transferase