Sandboxjg: Difference between revisions
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<Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /> | <Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /> | ||
The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein in Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to regulate cell volume. | The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein in Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to regulate cell volume. | ||
Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+ | Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+. | ||
The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane. Its structure allows it to use electrostatic interactions with the dipoles of the α-helices and with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore. | The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane. Its structure allows it to use electrostatic interactions with the dipoles of the α-helices and with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore. | ||
