Sandbox GGC7: Difference between revisions

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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.

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 ~~<ref>doi: 10.1038/nature05143</ref>~~.

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.

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.

Sandbox GGC7: Difference between revisions

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 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.
-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 <ref>doi: 10.1038/nature05143</ref>.
+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.
 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.