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: https://doi.org/10.2174/092986607779117173

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.

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