Sandbox Reserved 1441
From Proteopedia
(Difference between revisions)
(New page: {{Sandbox_MedChem-StOlaf_Hanson}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' ...) |
|||
Line 1: | Line 1: | ||
{{Sandbox_MedChem-StOlaf_Hanson}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_MedChem-StOlaf_Hanson}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
- | + | Active Site of Dipeptidyl Peptidase IV (DPP-IV) | |
+ | |||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <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 < 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. | ||
- | + | 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. | |
- | + | ||
- | + |
Revision as of 17:46, 29 January 2018
This Sandbox is Reserved from 5 Jan through 7 Feb, 2018 for use in the course Medicinal Chemistry taught by Bob Hanson at the St. Olaf College, Northfield, MN. This reservation includes Sandbox Reserved 1431 through Sandbox Reserved 1445. |
To get started:
More help: Help:Editing |
Active Site of Dipeptidyl Peptidase IV (DPP-IV)
|