Sandbox Wabash09
From Proteopedia
| Line 1: | Line 1: | ||
Composed By:Cameron Brown | Composed By:Cameron Brown | ||
| + | |||
| + | ==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. If mutations occur at R117, R334, and R347, then the ion gate is 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. | ||
==The Mechanism of Trypsin== | ==The Mechanism of Trypsin== | ||
<StructureSection load='2agg' size='340' side='right' caption='Intermediate of Trypsin catalyzed hydrolysis' scene=''> | <StructureSection load='2agg' size='340' side='right' caption='Intermediate of Trypsin catalyzed hydrolysis' scene=''> | ||
| Line 8: | Line 14: | ||
| - | </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. If mutations occur at R117, R334, and R347, then the ion gate is 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 a phosphorylation reaction that provides the energy necessary to move chloride ions though the channel. Mutations at these sites would prevent phosphorylation from supplying the energy needed for the functioning of the ion channel. | ||
<references /> | <references /> | ||
<ref>PMID:16636277</ref> | <ref>PMID:16636277</ref> | ||
<ref>Fundamentals of Biochemistry 3rd Ed.</ref> | <ref>Fundamentals of Biochemistry 3rd Ed.</ref> | ||
Revision as of 14:41, 15 April 2016
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. If mutations occur at R117, R334, and R347, then the ion gate is 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
| |||||||||||
