Sandbox Reserved 1442: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 6: Line 6:


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.
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.
<jmol><jmollink><text>View Figure 1a: Overall view of the µ-OR structure</text><script>exit;figure=1;SCRIPT "http://proteopedia.org/wiki/images/a/a6/Animation1.png"</script></jmollink></jmol>
Shown in Figure 1a is a close-up view of a morphinan antagonist ([https://chemapps.stolaf.edu/jmol/jmol.php?pdbid=BF0&script=set%20echo%20top%20left;echo%20PDBid%20BF0;spin%20on PDBid BF0]) bound to the µ-opioid receptor. The green circles indicate hydrogen bonds.
<jmol><jmollink><text>Animate Figure 1a</text><script>script "http://proteopedia.org/wiki/images/1/12/Transition2.spt"</script></jmollink></jmol>
</St

Revision as of 16:52, 30 January 2018

Dipeptidyl Peptidase IV (DPP-IV)

Active Site of Dipeptidyl Peptidase IV (DPP-IV)

<StructureSection load='1nu6' size='340' side='right' caption='Dipeptidyl Peptidase IV' scene=>

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.

Retrieved from "https://proteopedia.org/index.php?title=Sandbox_Reserved_1442&oldid=2851266"