Molecular architecture of a retinal cGMP-gated channel: the arrangement of the cytoplasmic domains
AUTOR(ES)
Higgins, Matthew K.
FONTE
Oxford University Press
RESUMO
Cyclic nucleotide-gated (CNG) channels play a central role in the conversion of sensory information, such as light and scent, into primary electrical signals. We have purified the CNG channel from bovine retina and have studied it using electron microscopy and image processing. We present the structure of the channel to 35Å resolution. This three-dimensional reconstruction provides insight into the architecture of the protein, suggesting that the cyclic nucleotide-binding domains, which initiate the response to ligand, ‘hang’ below the pore-forming part of the channel, attached by narrow linkers. The structure also suggests that the four cyclic nucleotide-binding domains present in each channel form two distinct domains, lending structural weight to the suggestion that the four subunits of the CNG channels are arranged as a pair of dimers.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125374Documentos Relacionados
- Ca2+ modulation of the cGMP-gated channel of bullfrog retinal rod photoreceptors.
- Primary structure and functional expression of a cGMP-gated potassium channel.
- The multi-ion nature of the cGMP-gated channel from vertebrate rods.
- Diacylglycerol analogs inhibit the rod cGMP-gated channel by a phosphorylation-independent mechanism.
- Block of the cGMP-gated cation channel of catfish rod and cone photoreceptors by organic cations.