According to his new duopapers with Steve Long in Science, The shaker type Kv1.2 Potassium channel structure has been solved down to 2.9 A resolution which also give us some glim of how the voltage gated potassium channel works.
The contradiction of the sensor movement is in a very big argument. I just waded through his papers a couple times without really concentrating myself reading them.
However, the structure is really beautiful and the crystal packing seems to have a lot less contraint than the KvAP. Even if Steve add back the magic mixture of lipid into the crystal trial, the final structure doesnt show any density of the lipid at all which will leave a mystery if the crystal packing still effects the transmembrane part of the protein becasue of
- There is a tremendous space between the pore domains in the crystal which is likely to be filled with lipid However, this may not be a big issue because it is also possible that the lipid itself is too fexible to be able to resolved any structure by diffraction.
- The pore domain still interact with Beta region of another Kv1.2 channel which may somehow distort the orientation of the flexible helices in the crystal but this shouldnot be a problem either.
Well! this structure indeed give us an enormous information about the eukaryotic potassium channel and provides a lot of insight into the movement of the voltage sensor of the famous Shaker channel.
All I could say is that "his work is always extremely impressive"
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