Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-22278
Neuron 1993 Sep 01;113:459-66. doi: 10.1016/0896-6273(93)90150-p.
Show Gene links Show Anatomy links

Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel.

Root MJ , MacKinnon R .


???displayArticle.abstract???
Divalent cation blockade of cGMP-gated channels in photoreceptor cells ensures the low open channel noise required for a highly sensitive visual transduction process. This study identifies a divalent cation-binding site in the pore of a retinal cGMP-gated channel expressed in Xenopus oocytes. Substitution of a specific glutamate residue by a neutral amino acid renders the channel insensitive to external Mg2+ and Ca2+ and affects the conduction of Na+. The mutated channels remain sensitive to internal divalent cations. These results place the glutamate residue in the ion conduction pathway close to the extracellular surface.

???displayArticle.pubmedLink??? 7691102
???displayArticle.link??? Neuron
???displayArticle.grants??? [+]