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| | <StructureSection load='3t6j' size='340' side='right'caption='[[3t6j]], [[Resolution|resolution]] 2.98Å' scene=''> | | <StructureSection load='3t6j' size='340' side='right'caption='[[3t6j]], [[Resolution|resolution]] 2.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6J FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t6b|3t6b]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.976Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPP3, hDPPIII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_III Dipeptidyl-peptidase III], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.4 3.4.14.4] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6j OCA], [https://pdbe.org/3t6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6j RCSB], [https://www.ebi.ac.uk/pdbsum/3t6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6j ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6j OCA], [https://pdbe.org/3t6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6j RCSB], [https://www.ebi.ac.uk/pdbsum/3t6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DPP3_HUMAN DPP3_HUMAN]] Cleaves Arg-Arg-beta-naphthylamide.
| + | [https://www.uniprot.org/uniprot/DPP3_HUMAN DPP3_HUMAN] Cleaves Arg-Arg-beta-naphthylamide. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dipeptidyl-peptidase III]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bezerra, G A]] | + | [[Category: Bezerra GA]] |
| - | [[Category: Gruber, K]] | + | [[Category: Gruber K]] |
| - | [[Category: Domain motion]]
| + | |
| - | [[Category: Entropy binding]]
| + | |
| - | [[Category: Human dipeptidylpeptidase iii]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Opioid peptide complex]]
| + | |
| Structural highlights
Function
DPP3_HUMAN Cleaves Arg-Arg-beta-naphthylamide.
Publication Abstract from PubMed
Opioid peptides are involved in various essential physiological processes, most notably nociception. Dipeptidyl peptidase III (DPP III) is one of the most important enkephalin-degrading enzymes associated with the mammalian pain modulatory system. Here we describe the X-ray structures of human DPP III and its complex with the opioid peptide tynorphin, which rationalize the enzyme's substrate specificity and reveal an exceptionally large domain motion upon ligand binding. Microcalorimetric analyses point at an entropy-dominated process, with the release of water molecules from the binding cleft ("entropy reservoir") as the major thermodynamic driving force. Our results provide the basis for the design of specific inhibitors that enable the elucidation of the exact role of DPP III and the exploration of its potential as a target of pain intervention strategies.
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III.,Bezerra GA, Dobrovetsky E, Viertlmayr R, Dong A, Binter A, Abramic M, Macheroux P, Dhe-Paganon S, Gruber K Proc Natl Acad Sci U S A. 2012 Apr 24;109(17):6525-30. Epub 2012 Apr 9. PMID:22493238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bezerra GA, Dobrovetsky E, Viertlmayr R, Dong A, Binter A, Abramic M, Macheroux P, Dhe-Paganon S, Gruber K. Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III. Proc Natl Acad Sci U S A. 2012 Apr 24;109(17):6525-30. Epub 2012 Apr 9. PMID:22493238 doi:10.1073/pnas.1118005109
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