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==Structure of human DPPIII in complex with the opioid peptide Tynorphin, at 2.4 Angstroms== | |||
<StructureSection load='3t6b' size='340' side='right' caption='[[3t6b]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t6b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T6B FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t6j|3t6j]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPP3, hDPPIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_III Dipeptidyl-peptidase III], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t6b RCSB], [http://www.ebi.ac.uk/pdbsum/3t6b PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== | ==See Also== | ||
*[[Dipeptidyl peptidase|Dipeptidyl peptidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dipeptidyl-peptidase III]] | [[Category: Dipeptidyl-peptidase III]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bezerra, G A | [[Category: Bezerra, G A]] | ||
[[Category: Gruber, K | [[Category: Gruber, K]] | ||
[[Category: Domain motion]] | [[Category: Domain motion]] | ||
[[Category: Entropy binding]] | [[Category: Entropy binding]] | ||
Revision as of 09:45, 21 December 2014
Structure of human DPPIII in complex with the opioid peptide Tynorphin, at 2.4 AngstromsStructure of human DPPIII in complex with the opioid peptide Tynorphin, at 2.4 Angstroms
Structural highlights
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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