Sandbox GGC7: Difference between revisions
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==Insulin Protease (Insulin Degrading Enzyme)== | ==Insulin Protease (Insulin Degrading Enzyme)== | ||
<StructureSection load='2G54' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='2G54' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Insulin is a hormone that is secreted by the pancreas in response to an increased level of glucose in the blood, usually after a meal. Insulin stimulates the muscles and adipose tissue to take up and store the excess glucose. When the concentration of glucose in the blood drops, insulin is no longer needed and an insulin-degrading enzyme is produced in order to reduce the amount of insulin in the body. | Insulin is a hormone that is secreted by the pancreas in response to an increased level of glucose in the blood, usually after a meal. Insulin stimulates the muscles and adipose tissue to take up and store the excess glucose. Insulin is a dipeptide that contains a A and B chain. The A chain has an N-terminal helix linked to an anti-parallel C-terminal helix. The B chain has a central helical segment. The two chains are connected by 2 di-sulphide bonds that join the N- and C-terminal helices of the A chain to the central helix of the B chain <ref>PMID: 16278749</ref> . When the concentration of glucose in the blood drops, insulin is no longer needed and an insulin-degrading enzyme is produced in order to reduce the amount of insulin in the body. | ||
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== | == Structure == | ||
The insulin-degrading enzyme (IDE) is a highly conserved protease that uses zinc (Zn2+) as a cofactor in breaking down insulin and amyloid beta-proteins <ref>doi: 10.1038/nature05143</ref>. The structure of IDE is a monomer with two N-terminal domains, which forms the catalytic site and two C-terminal domains that facilitates the substrate binding. The N-terminal domains are connected to the C-terminal domains via a 28-residue loop that forms a chamber that is shaped like a triangular prism. | The insulin-degrading enzyme (IDE) is a highly conserved protease that uses zinc (Zn2+) as a cofactor in breaking down insulin and amyloid beta-proteins <ref>doi: 10.1038/nature05143</ref>. The structure of IDE is a monomer with two N-terminal domains, which forms the catalytic site and two C-terminal domains that facilitates the substrate binding. The N-terminal domains are connected to the C-terminal domains via a 28-residue loop that forms a chamber that is shaped like a triangular prism. | ||
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In the open conformation, the insulin protein enters the enzyme opening causing a conformational change that allows the enzyme to fully recognize the protein and catalyzes protein degradation. | In the open conformation, the insulin protein enters the enzyme opening causing a conformational change that allows the enzyme to fully recognize the protein and catalyzes protein degradation. | ||
== Function == | |||
== Disease == | == Disease == | ||
