1MCV

Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase

Summary for 1MCV

• Entry DOI: 10.2210/pdb1mcv/pdb
• Related: 1PPE 1PPF 1QNJ
• Descriptor: Elastase 1, HEI-TOE I, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: elastase-inhibitor complex, hybrid squash inhibitor, hydrolase
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted: P00772
• Total number of polymer chains: 2
• Total formula weight: 29038.61

Authors

Ay, J.,Hilpert, K.,Krauss, N.,Schneider-Mergener, J.,Hoehne, W. (deposition date: 2002-08-06, release date: 2003-02-04, Last modification date: 2024-11-13)

Primary citation

Ay, J.,Hilpert, K.,Krauss, N.,Schneider-Mergener, J.,Hohne, W.
Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution.
Acta Crystallogr.,Sect.D, 59:247-254, 2003

PubMed Abstract: The crystal structure of porcine pancreatic elastase in complex with a hybrid squash inhibitor (HEI-TOE I; 28 amino acids) has been determined to a resolution of 1.8 A. To construct the hybrid inhibitor, the trypsin-binding loop of the squash inhibitor from Ecballium elaterium was substituted by the sequence of a peptide that was derived from the third domain of the turkey ovomucoid inhibitor and was optimized to inhibit porcine pancreatic elastase. This modification of the squash inhibitor changed its specificity for trypsin to a specificity for porcine pancreatic elastase. Specific interactions of this hybrid inhibitor with porcine pancreatic elastase and the differences from the interactions of the ovomucoid inhibitor with human leukocyte elastase are discussed. The binding loop of the inhibitor adopts a 'canonical' conformation and the scissile bond Leu-Glu remains intact.

PubMed: 12554935
DOI: 10.1107/S0907444902020887

Experimental method

X-RAY DIFFRACTION (1.8 Å)