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Crystallization and Preliminary Diffraction Studies of Porcine Pancreatic Elastase in Complex with a Novel Inhibitor

Oliveira, Tânia F.; Mulchande, Jalmira; Moreira, Rui; Iley, Jim and Archer, Margarida (2007). Crystallization and Preliminary Diffraction Studies of Porcine Pancreatic Elastase in Complex with a Novel Inhibitor. Protein and Peptide Letters, 14(1) pp. 93–95.

DOI (Digital Object Identifier) Link: http://dx.doi.org/10.2174/092986607779117173
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Abstract

Porcine pancreatic elastase (PPE) was crystallized in complex with a novel inhibitor at pH 5 and X-ray diffraction data were collected at a synchrotron source to 1.66 Å. Crystals belong to the orthorhombic space group P212121, with unit cell parameters a = 50.25 Å, b = 57.94 Å and c = 74.69 Å. PPE is often used as model for drug target, due to its structural homology with the important therapeutic target human leukocyte elastase (HLE). Elastase is a serine protease that belongs to the chymotrypsin family, which has the ability to degrade elastin, an important component in connective tissues. Excessive elastin proteolysis leads to a number of pathological diseases.

Item Type: Journal Article
ISSN: 0929-8665
Keywords: human leukocyte elastase; porcine pancreatic elastase; beta-lactam inhibitors; crystallization
Academic Unit/Department: Science > Life, Health and Chemical Sciences
Item ID: 5976
Depositing User: James Iley
Date Deposited: 18 Apr 2007
Last Modified: 02 Dec 2010 19:55
URI: http://oro.open.ac.uk/id/eprint/5976
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