Sandbox GGC7: Difference between revisions
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== Structure == | == Structure == | ||
The structure of IDE is a <scene name='75/752270/Ide_homodimer/1'>homodimer</scene> with two N-terminal domains, which forms the catalytic site and two C-terminal domains that facilitates the substrate binding <ref>DOI 10.1074/jbc.M900068200</ref>. 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 structure of IDE is a <scene name='75/752270/Ide_homodimer/1'>homodimer</scene> with two N-terminal domains, which forms the catalytic site and two C-terminal domains that facilitates the substrate binding <ref>DOI 10.1074/jbc.M900068200</ref>. 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 <scene name='75/752270/Ide_monomer/1'>metal binding site</scene> with two histidine's and one glutamine(his 108, his 112 and glu 198), the <scene name='75/752270/Ide_atp_binding-active_sites/1'>active site</scene> of a glutamine (Glu 111), ATP binding site (Arg 429) 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. | Domain 1 houses the <scene name='75/752270/Ide_monomer/1'>metal binding site</scene> with two histidine's and one glutamine(his 108, his 112 and glu 198), the <scene name='75/752270/Ide_atp_binding-active_sites/1'>active site</scene> of a glutamine (Glu 111), ATP binding site (Arg 429) 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. | ||
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== Function == | == Function == | ||
Once the insulin molecule enters the active site and is recognized, the enzyme changes conformation from the open state to the closed state and begins to unfold the insulin and makes initial cleavages in the middle of both the A and B chains. | Once the insulin molecule enters the active site and is recognized, ATP binds to the appropriate site and the enzyme changes conformation from the open state to the closed state and begins to unfold the insulin and makes two initial cleavages, one each in the middle of both the A and B chains. The enzyme then makes six more cleavages. One cleavage site right next to the first one on the A chain and 5 more on the B chain <ref>DOI 10.1074/jbc.M900068200</ref>. Three near the middle and two near the C-terminus. There are no cleavage sites that are near the N-terminus of either chain. | ||
== Disease == | == Disease == | ||
