Chloride ion channel strikingly different from potassium kin

"Why did nature come up with such a structural plan?" ask Rockefeller University professor Roderick MacKinnon and colleagues in their Jan. 17 Nature cover article describing the three-dimensional structure of a type of chloride channel called the ClC.

The high-resolution crystallographic images published in Nature represent another instance of the Rockefeller scientists remarkable knack for visualizing the specialized proteins that provide ports of cellular entry for potassium, sodium, calcium and chloride.

MacKinnon, who is a Howard Hughes Medical Institute investigator, leads a scientific team that is adding unprecedented detail to existing descriptions of the chloride ion channel.

The research findings are seminal for what is bound to be an industry in developing drug targets for ion channel impairments. The ClC chloride channel, which is found in organisms from bacteria to humans, is linked with some heritable diseases of the muscles and kidney. Mutations in another kind of chloride channel, called the CFTR, are responsible for cystic fibrosis, the most common genetic disease in Caucasian populations.

There are many varieties of ion channels. A cousin to the chloride channel, the potassium ion channel, was structurally solved by MacKinnons group in 1998. Numerous existing drugs are known to trigger changes to the potassium ion channel, causing a potentially fatal heart disorder called Long QT syndrome. Developing biomedical solutions to the known impairments of ion channels will improve human health considerably.

The channels, also called transmembrane proteins, ingeniously shepherd vital molecules across cellular and intracellular membranes, keeping surrounding structures and biochemistry intact. Each kind of ion channel has selective features that permit only appropriately sized and charged molecules to travel to th
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Contact: Lynn Love
lovel@mail.rockefeller.edu
212-327-8977
Rockefeller University
18-Jan-2002