Sandboxjg
From Proteopedia
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Roderick MacKinnon and his team determined the structure of the protein and concluded that it was a channel. In a 2004 article co-authored by Accardi and Miller, it was established that the protein functioned by means of a 2:1 chloride ion-hydrogen ion exchange mechanism. | Roderick MacKinnon and his team determined the structure of the protein and concluded that it was a channel. In a 2004 article co-authored by Accardi and Miller, it was established that the protein functioned by means of a 2:1 chloride ion-hydrogen ion exchange mechanism. | ||
| - | The CLC-ec1 transporter is a protein dimer made up of two functional antiparallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helic dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chains functions independently, we will focus on the structure of one pore. | + | The CLC-ec1 transporter is a protein dimer made up of two functional antiparallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helic dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chains functions independently, we will focus on the structure of one pore. |
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| + | To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene> | ||
| + | <scene name='Sandboxjg/1ots/2'>Hi Hi</scene> | ||
Revision as of 19:43, 13 June 2011
ClC Transporter
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The CLC-ec1 (1OTS) protein is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential to proper electrical activity in muscle cells and some neurons, in the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.
Roderick MacKinnon and his team determined the structure of the protein and concluded that it was a channel. In a 2004 article co-authored by Accardi and Miller, it was established that the protein functioned by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.
The CLC-ec1 transporter is a protein dimer made up of two functional antiparallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helic dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chains functions independently, we will focus on the structure of one pore.
To see the test
