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Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic ElastaseCrystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase
Structural highlights
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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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