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.
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Function
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 [3]. 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.
Domain 1 houses the active site with two histidine's (his 108 and his 112), one glutamate (Glu 189) and the Zn2+ ion cofactor. Several residues of domains 1 & 4 create a polar area of the triangular cavity, while residues of domains 2 & 3 create a nonpolar region of the cavity [4].
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.
Disease
Relevance
Structural highlights
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