3eq7: Difference between revisions

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-{{Seed}}
-[[Image:3eq7.png|left|200px]]
-<!--
+==Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors==
-The line below this paragraph, containing "STRUCTURE_3eq7", creates the "Structure Box" on the page.
+<StructureSection load='3eq7' size='340' side='right'caption='[[3eq7]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3eq7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EQ7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=X99:2-{3-[(2S)-4,4-DIFLUORO-2-(PYRROLIDIN-1-YLCARBONYL)PYRROLIDIN-1-YL]-3-OXOPROPYL}-ISOINDOLE-1,3(2H)-DIONE'>X99</scene></td></tr>
-{{STRUCTURE_3eq7|  PDB=3eq7  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eq7 OCA], [https://pdbe.org/3eq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eq7 RCSB], [https://www.ebi.ac.uk/pdbsum/3eq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eq7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
+== 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/eq/3eq7_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=3eq7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Three novel, N-acyl-pro-pyrrolidine-type, inhibitors of prolyl oligopeptidase (POP) with nanomolar activities were synthesized and their binding analyzed to the host enzyme in the light of X-ray diffraction and molecular modeling studies. We were interested in the alteration in the binding affinity at the S3 site as a function of the properties of the N-terminal group of the inhibitors. Our studies revealed that, for inhibitors with flat aromatic terminal groups, the optimal length of the linker chain is three C-C bonds, but this increases to four C-C bonds if there is a bulky group in the terminal position. Molecular dynamics calculations indicate that this is due to the better fit into the binding pocket. A 4-fold enhancement of the inhibitor activity upon replacement of the 4-CH2 group of the proline ring by CF2 is a consequence of a weak hydrogen bond formed between the fluorine atom and the hydroxy group of Tyr473 of the host enzyme. There is notably good agreement between the calculated and experimental free energies of binding; the average error in the IC50 values is around 1 order of magnitude.
-===Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors===
+Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules.,Kanai K, Aranyi P, Bocskei Z, Ferenczy G, Harmat V, Simon K, Batori S, Naray-Szabo G, Hermecz I J Med Chem. 2008 Dec 11;51(23):7514-22. PMID:19006380<ref>PMID:19006380</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3eq7" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-EQ7 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQ7 OCA].
+*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:19006380</ref><references group="xtra"/>
+__TOC__
-[[Category: Prolyl oligopeptidase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Aranyi, P.]]
+[[Category: Aranyi P]]
-[[Category: Bocskei, Z.]]
+[[Category: Bocskei Z]]
-[[Category: Ferenczy, G.]]
+[[Category: Ferenczy G]]
-[[Category: Harmat, V.]]
+[[Category: Harmat V]]
-[[Category: Hermecz, I.]]
+[[Category: Hermecz I]]
-[[Category: Kanai, K.]]
+[[Category: Kanai K]]
-[[Category: Naray-Szabo, G.]]
+[[Category: Naray-Szabo G]]
-[[Category: Simon, K.]]
+[[Category: Simon K]]
-[[Category: Cytoplasm]]
-[[Category: Hydrolase]]
-[[Category: Protease]]
-[[Category: Protease-inhibitor complex]]
-[[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 16:46:07 2009''