Sandbox Reserved 1442: Difference between revisions

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==Crystal structure of the µ-opioid receptor bound to a morphinan antagonist==
==Dipeptidyl Peptidase IV (DPP-IV)==




[https://www.nature.com/articles/nature10954 Nature volume 485, pages 321–326 (17 May 2012)
{{Sandbox_MedChem-StOlaf_Hanson}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
doi:10.1038/nature10954]
 
 
'''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.


<StructureSection load='' size='340' side='right' caption='Click a green link on the left to load Figure 1' scene=''>


<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>
<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>
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