Sandbox GGC7: Difference between revisions

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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 active site 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.

There are two conformations for the enzyme, open and closed. 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 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 active site 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.
 There are two conformations for the enzyme, open and closed.  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.