Sickly channels in mild disease

Article Abstract:

Cystic fibrosis is caused by a defective epithelial Cl- channel, the cystic fibrosis transmembrane regulator (CFTR). The most common mutation on the CFTR gene involves deletion of F508 in one of the two nucleotide-binding domains. Three less common mutations that lead to mild forms of the disease have also been studied. These involve missense mutations each altering a different arginine residue. However, it was found that the clinically severest mutant CFTR gene is much more prevalent than the less harmful variants. It is speculated that a deficiency in epithelial fluid secretion would ameliorate the severity of dehydration due to enterotoxin-slicited diarrhea.

Cystic fibrosis, Mutagenesis, Chloride channels

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Cuddling up to channel activation

Article Abstract:

An innovative technique allows researchers to analyse the functions of an allosteric membrane protein and the behaviour of a single cyclic nucleotide-gated ion channel. The experiment also shows the effects of ligands locked onto the channel's four identical cGMP-binding sites. Results of the study are discussed.

Ligand binding (Biochemistry), Allosteric proteins, Nucleotides

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Shake, rattle or roll?

Article Abstract:

A remarkable property of the voltage sensor that sharpens one's view of its transmembrane movement is described. The controversy regarding the movement of the voltage sensor is also discussed.

United States, Science & research, Nervous system, Membrane proteins

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