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

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

Volume: 14 Issue: 1

Author(s): Tania F. Oliveira, Jalmira Mulchande, Rui Moreira, Jim Iley and Margarida Archer

Affiliation:

Keywords: Human leukocyte elastase, Porcine pancreatic elastase, β-Lactams inhibitors, Crystallization

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.

Cite this article as:

Oliveira F. Tania, Mulchande Jalmira, Moreira Rui, Iley Jim and Archer Margarida, Crystallization and Preliminary Diffraction Studies of Porcine Pancreatic Elastase in Complex with a Novel Inhibitor, Protein & Peptide Letters 2007; 14 (1) . https://dx.doi.org/10.2174/092986607779117173