1H9L
PORCINE PANCREATIC ELASTASE COMPLEXED WITH ACETYL-VAL-GLU-PRO-ILE-COOH
Summary for 1H9L
| Entry DOI | 10.2210/pdb1h9l/pdb |
| 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 |
| Descriptor | PEPTIDE INHIBITOR, ELASTASE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | serine proteinase, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | SUS SCROFA (PIG) More |
| Total number of polymer chains | 2 |
| Total formula weight | 26546.74 |
| Authors | Wright, P.A.,Wilmouth, R.C.,Clifton, I.J.,Schofield, C.J. (deposition date: 2001-03-13, release date: 2001-11-27, Last modification date: 2024-10-16) |
| Primary citation | Wright, P.A.,Wilmouth, R.C.,Clifton, I.J.,Schofield, C.J. Kinetic and Crystallographic Analysis of Complexes Formed between Elastase and Peptides from Beta-Casein Eur.J.Biochem., 268:2969-, 2001 Cited by PubMed Abstract: 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. PubMed: 11358514DOI: 10.1046/J.1432-1327.2001.02186.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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