User:Amy Kerzmann/Sandbox 2
From Proteopedia
(→Voltage-gated Potassium Channel) |
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== Voltage-gated Potassium Channel == | == Voltage-gated Potassium Channel == | ||
| + | {{STRUCTURE_3cs9| PDB=1bl8 | SCENE=User:Amy_Kerzmann/Sandbox_2/Potassium_ions/2}} | ||
'''Backgound''' | '''Backgound''' | ||
---- | ---- | ||
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| - | + | '''Channel Structure:''' | |
| + | ---- | ||
| + | The potassium channel is a homotetramer. The central core of this protein is comprised of eight helices, two from each monomeric subunit. Since all monomers have the same orientation in the membrane, the protein has a four-fold rotational symmetry when viewed from the membrane surface. As a result, each of the channel-lining residues appears as a ring of four identical sidechains. This principle is represented by the conserved <scene name='User:Amy_Kerzmann/Sandbox_2/Tyrosine_symmetry/1'>tyrosine</scene> residues that function as selectivity filters within the cavity. Additional <scene name='User:Amy_Kerzmann/Sandbox_2/Aspartate_symmetry/1'>aspartate</scene> and <scene name='User:Amy_Kerzmann/Sandbox_2/Threonine_symmetry/2'>threonine</scene> residues line the channel. Looking at a <scene name='User:Amy_Kerzmann/Sandbox_2/Channel-lining_residues/1'>composite</scene> of these residues, one can see that some hydrophobic patches remain within the cavity. | ||
| - | + | <applet load='1bl8' size='300' frame='true' align='left' caption='First Crystal Structure of a Potassium Channel. (PDB 1bl8)' /> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | Channel Function: | + | '''Channel Function:''' |
---- | ---- | ||
Here's how it works. | Here's how it works. | ||
Revision as of 20:47, 24 September 2009
Voltage-gated Potassium Channel
Template:STRUCTURE 3cs9 Backgound
This crystal structure illuminated the principles of ion selectivity when it was solved in 1998.[1] To further demonstrate the importance of this structure, the 2003 Nobel Prize in Chemistry was awarded to the principal investigator, Roderick MacKinnon.
Channel Structure:
The potassium channel is a homotetramer. The central core of this protein is comprised of eight helices, two from each monomeric subunit. Since all monomers have the same orientation in the membrane, the protein has a four-fold rotational symmetry when viewed from the membrane surface. As a result, each of the channel-lining residues appears as a ring of four identical sidechains. This principle is represented by the conserved residues that function as selectivity filters within the cavity. Additional and residues line the channel. Looking at a of these residues, one can see that some hydrophobic patches remain within the cavity.
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Channel Function:
Here's how it works.
References
