Sandbox Wabash09
From Proteopedia
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==CFTR HOMEWORK== | ==CFTR HOMEWORK== | ||
| - | This <scene name='72/725331/Cftr_conductance/1'>structure</scene> depicts the amino acid residues in mutation sites that affect the conductance of CFTR in cystic fibrosis. These residues are located near the connection of the two amino acid chains that form the quaternary structure of the protein. A possible reason why these mutations affect the ability of CFTR to conduct chloride ions through the channel is because these residues are important in the opening of the channel. | + | This <scene name='72/725331/Cftr_conductance/1'>structure</scene> depicts the amino acid residues in mutation sites that affect the conductance of CFTR in cystic fibrosis. These residues are located near the connection of the two amino acid chains that form the quaternary structure of the protein. A possible reason why these mutations affect the ability of CFTR to conduct chloride ions through the channel is because these residues are important in the opening of the channel. The specific tertiary and quaternary shifts are no longer correct if mutations occur at R117, R334, and R347. the ion gate is therefore no longer able to open as effectively due to the changes in residue properties. |
This <scene name='72/725331/Cftr_regulation/1'>structure</scene> also highlights the residues that mutate in cystic fibrosis to affect the regulation of CFTR. These residues are located on both ends of the amino chains which are opposite the ends with the amino acid residues discussed in conductance mutations. A possible reason why mutations at these specific residues cause regulation issues is that these residues are involved in the binding that leads to the structural shift that opens the channel. If regulators are not able to bind to these specific residues after mutation, allowing the opening and closing of the ion channel, then the passage of chloride ions can not be regulated by the cell. | This <scene name='72/725331/Cftr_regulation/1'>structure</scene> also highlights the residues that mutate in cystic fibrosis to affect the regulation of CFTR. These residues are located on both ends of the amino chains which are opposite the ends with the amino acid residues discussed in conductance mutations. A possible reason why mutations at these specific residues cause regulation issues is that these residues are involved in the binding that leads to the structural shift that opens the channel. If regulators are not able to bind to these specific residues after mutation, allowing the opening and closing of the ion channel, then the passage of chloride ions can not be regulated by the cell. | ||
Current revision
Composed By:Cameron Brown
CFTR HOMEWORK
This depicts the amino acid residues in mutation sites that affect the conductance of CFTR in cystic fibrosis. These residues are located near the connection of the two amino acid chains that form the quaternary structure of the protein. A possible reason why these mutations affect the ability of CFTR to conduct chloride ions through the channel is because these residues are important in the opening of the channel. The specific tertiary and quaternary shifts are no longer correct if mutations occur at R117, R334, and R347. the ion gate is therefore no longer able to open as effectively due to the changes in residue properties.
This also highlights the residues that mutate in cystic fibrosis to affect the regulation of CFTR. These residues are located on both ends of the amino chains which are opposite the ends with the amino acid residues discussed in conductance mutations. A possible reason why mutations at these specific residues cause regulation issues is that these residues are involved in the binding that leads to the structural shift that opens the channel. If regulators are not able to bind to these specific residues after mutation, allowing the opening and closing of the ion channel, then the passage of chloride ions can not be regulated by the cell.
The Mechanism of Trypsin
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