User:Amy Kerzmann/Sandbox 2

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'''Backgound'''
'''Backgound'''
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This crystal structure illuminated the principles of ion selectivity when it was solved in 1998.<ref>PMID:9525859</ref> To further demonstrate the importance of this structure, the [[http://nobelprize.org/nobel_prizes/chemistry/laureates/2003 2003 Nobel Prize in Chemistry]] was awarded to the principal investigator, Roderick MacKinnon.
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This crystal structure illuminated the principles of ion selectivity when it was solved in 1998.<ref>PMID:9525859</ref> To further demonstrate the importance of this structure, the [http://nobelprize.org/nobel_prizes/chemistry/laureates/2003 2003 Nobel Prize in Chemistry] was awarded to the principal investigator, Roderick MacKinnon.
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Channel Structure:
Channel Structure:
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The potassium channel of influenza A is a homotetramer. The central core of this protein is comprised of four transmembrane helices, one 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_1/Conserved_his_and_trp/3'>tryptophan and histidine</scene> residues that function as proton gates within the cavity.
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The potassium channel of influenza A is a homotetramer. The central core of this protein is comprised of four transmembrane helices, one 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/Channel-lining_residues/1'>TextToBeDisplayed</scene> residues that function as selectivity filters within the cavity.

Revision as of 16:51, 23 September 2009

Voltage-gated Potassium Channel

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.


First Crystal Structure of a Potassium Channel. (PDB 1bl8)

Drag the structure with the mouse to rotate


Channel Structure:

The potassium channel of influenza A is a homotetramer. The central core of this protein is comprised of four transmembrane helices, one 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.


Channel Function:

Here's how it works.


References

  1. ↑ Doyle DA, Morais Cabral J, Pfuetzner RA, Kuo A, Gulbis JM, Cohen SL, Chait BT, MacKinnon R. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science. 1998 Apr 3;280(5360):69-77. PMID:9525859

Proteopedia Page Contributors and Editors (what is this?)

Amy Kerzmann, Jaime Prilusky

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