1mcv
From Proteopedia
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase
Overview
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.
About this Structure
1MCV is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution., Ay J, Hilpert K, Krauss N, Schneider-Mergener J, Hohne W, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):247-54. Epub 2003, Jan 23. PMID:12554935
Page seeded by OCA on Thu Mar 20 12:42:00 2008
