1h9l
From Proteopedia
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| - | [[Image:1h9l.jpg|left|200px]]<br /><applet load="1h9l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h9l, resolution 1.67Å" /> | ||
| - | '''PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH'''<br /> | ||
| - | == | + | ==PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH== |
| - | + | <StructureSection load='1h9l' size='340' side='right'caption='[[1h9l]], [[Resolution|resolution]] 1.67Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [[ | + | <table><tr><td colspan='2'>[[1h9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H9L 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]] 1.67Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1h9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9l OCA], [https://pdbe.org/1h9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h9l RCSB], [https://www.ebi.ac.uk/pdbsum/1h9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9l ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin. |
| - | [ | + | == 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/h9/1h9l_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h9l ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human beta-casomorphin-7 (NH2-Tyr-Pro-Phe-Val-Glu-Pro-Ile-CO2H) is a naturally occurring peptide inhibitor of elastase that has been shown to form an acyl-enzyme complex stable enough for X-ray crystallographic analysis at pH 5. To investigate the importance of the N-terminal residues of the beta-casomorphin-7 peptide for the inhibition of elastase, kinetic and crystallographic analyses were undertaken to identify the minimum number of residues required for effective formation of a stable complex between truncated beta-casomorphin-7 peptides and porcine pancreatic elastase (PPE). The results clearly demonstrate that significant inhibition of PPE can be effected by simple tri-, tetra-and pentapeptides terminating in a carboxylic acid. These results also suggest that in vivo regulation of protease activity could be mediated via short peptides as well as by proteins. Crystallographic analysis of the complex formed between N-acetyl-Val-Glu-Pro-Ile-CO2H and PPE at pH 5 (to 1.67 A resolution) revealed an active site water molecule in an analogous position to that observed in the PPE/beta-casomorphin-7 structure supportive of its assignment as the 'hydrolytic water' in the deacylation step of serine protease catalysis. | ||
| - | + | Kinetic and crystallographic analysis of complexes formed between elastase and peptides from beta-casein.,Wright PA, Wilmouth RC, Clifton IJ, Schofield CJ Eur J Biochem. 2001 May;268(10):2969-74. PMID:11358514<ref>PMID:11358514</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1h9l" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Elastase 3D structures|Elastase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sus scrofa]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Clifton IJ]] | ||
| + | [[Category: Schofield CJ]] | ||
| + | [[Category: Wilmouth RC]] | ||
| + | [[Category: Wright PA]] | ||
Current revision
PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH
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