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1h9l

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Revision as of 06:40, 10 September 2015

PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH

Structural highlights

1h9l is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1hv7, 1inc, 1jim, 1lvy, 1nes, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est
Activity:	Pancreatic elastase, with EC number 3.4.21.36
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CELA1_PIG] Acts upon elastin.

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wright PA, Wilmouth RC, Clifton IJ, Schofield CJ. Kinetic and crystallographic analysis of complexes formed between elastase and peptides from beta-casein. Eur J Biochem. 2001 May;268(10):2969-74. PMID:11358514

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h9l"

@@ Line 7: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0e|1b0e]], [[1bma|1bma]], [[1btu|1btu]], [[1c1m|1c1m]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1est|1est]], [[1fle|1fle]], [[1hv7|1hv7]], [[1inc|1inc]], [[1jim|1jim]], [[1lvy|1lvy]], [[1nes|1nes]], [[1qgf|1qgf]], [[1qix|1qix]], [[1qnj|1qnj]], [[1qr3|1qr3]], [[2est|2est]], [[3est|3est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </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=1h9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h9l RCSB], [http://www.ebi.ac.uk/pdbsum/1h9l PDBsum]</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=1h9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9l OCA], [http://pdbe.org/1h9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h9l RCSB], [http://www.ebi.ac.uk/pdbsum/1h9l PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1h9l" style="background-color:#fffaf0;"></div>
 ==See Also==

1h9l

From Proteopedia

Revision as of 06:40, 10 September 2015

PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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