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< | ==Crystal structure of human Dipeptidyl Peptidase III== | ||
<StructureSection load='3fvy' size='340' side='right'caption='[[3fvy]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fvy]] is a 1 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=3FVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FVY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3fvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvy OCA], [https://pdbe.org/3fvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fvy RCSB], [https://www.ebi.ac.uk/pdbsum/3fvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fvy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DPP3_HUMAN DPP3_HUMAN] Cleaves Arg-Arg-beta-naphthylamide. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/3fvy_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fvy ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22493238</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3fvy" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith | [[Category: Large Structures]] | ||
[[Category: Bochkarev | [[Category: Arrowsmith CH]] | ||
[[Category: Bountra | [[Category: Bochkarev A]] | ||
[[Category: Cossar | [[Category: Bountra C]] | ||
[[Category: Crombet | [[Category: Cossar D]] | ||
[[Category: Dobrovetsky | [[Category: Crombet L]] | ||
[[Category: Dong | [[Category: Dobrovetsky E]] | ||
[[Category: Duncan | [[Category: Dong A]] | ||
[[Category: Edwards | [[Category: Duncan B]] | ||
[[Category: Edwards AM]] | |||
[[Category: Seitova | [[Category: Seitova A]] | ||
[[Category: Sundstrom | [[Category: Sundstrom M]] | ||
Latest revision as of 09:52, 6 September 2023
Crystal structure of human Dipeptidyl Peptidase IIICrystal structure of human Dipeptidyl Peptidase III
Structural highlights
FunctionDPP3_HUMAN Cleaves Arg-Arg-beta-naphthylamide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOpioid 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 AlsoReferences
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