Sandbox Reserved 1441: Difference between revisions

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{{Sandbox_MedChem-StOlaf_Hanson}}

~~==Your Heading Here~~ (~~maybe something like 'Structure'~~)==

Active Site of Dipeptidyl Peptidase IV (DPP-IV)

~~This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~

~~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.~~

~~== Function ==~~

~~== Disease ==~~

~~== Relevance ==~~

~~== Structural highlights ==~~

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</~~StructureSection>~~

The DPP-IV active site exists at the intersection of a α/β hydrolase domain and a β-propeller domain and consists of the catalytic triad and supporting residues. The catalytic triad is made up of a nucleophile, Serine630, a base, Histidine740, and an acid, Aspartate708. Also essential to the cleaving mechanism are two supporting residues, Tyr547 and Tyr631, that stabilize the oxyanion tetrahedral intermediate by forming hydrogen bonds with the oxyanion. In addition, there are anchoring residues that coordinate the carbonyl of the N-terminal amino acid residue of the substrate and align it for the nucleophilic attack by Ser630. These residues are Glu205, Glu206, Asn710, and Arg125.

~~== References ==~~

~~<references/>~~

Sandbox Reserved 1441: Difference between revisions

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@@ Line 1: / Line 1: @@
 {{Sandbox_MedChem-StOlaf_Hanson}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-==Your Heading Here (maybe something like 'Structure')==
+Active Site of Dipeptidyl Peptidase IV (DPP-IV)
 <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
-This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
-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.
-== Function ==
-== Disease ==
-== Relevance ==
-== Structural highlights ==
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
-</StructureSection>
+The DPP-IV active site exists at the intersection of a α/β hydrolase domain and a β-propeller domain and consists of  the catalytic triad and supporting residues. The catalytic triad is made up of a nucleophile, Serine630, a base, Histidine740, and an acid, Aspartate708. Also essential to the cleaving mechanism are two supporting residues, Tyr547 and Tyr631, that stabilize the oxyanion tetrahedral intermediate by forming hydrogen bonds with the oxyanion. In addition, there are anchoring residues that coordinate the carbonyl of the N-terminal amino acid residue of the substrate and align it for the nucleophilic attack by Ser630. These residues are Glu205, Glu206, Asn710, and Arg125.
-== References ==
-<references/>