Critical assessment of a proposed model of Shaker.
Detailed three-dimensional structures at atomic resolution are essential to understand how voltage-activated K(+) channels function. The X-ray crystallographic structure of the KvAP channel has offered the first view at atomic resolution of the molecular architecture of a voltage-activated K(+) channel. In the crystal, the voltage sensors are bound by monoclonal Fab fragments, which apparently induce a non-native conformation of the tetrameric channel. Thus, despite this significant advance our knowledge of the native conformation of a Kv channel in a membrane remains incomplete. Numerous results from different experimental approaches provide very specific constraints on the structure of K(+) channels in functional conformations. These results can be used to go further in trying to picture the native conformation of voltage-gated K(+) channels. However, the direct translation of all the available information into three-dimensional models is not straightforward and many questions about the structure of voltage-activated K(+) channels are still unanswered. Our aim in this review is to summarize the most important pieces of information currently available and to provide a critical assessment of the model of Shaker recently proposed by Lainé et al.
Lainé
Muriel
M
Rockefeller University, 1280 York Ave, New York, NY 10021, USA.
Papazian
Diane M
DM
Roux
Benoît
B
D000818:Animals; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D015221:Potassium Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D051637:Shaker Superfamily of Potassium Channels
D015221:Potassium Channels; D051637:Shaker Superfamily of Potassium Channels