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- Title
Crystallization and preliminary diffraction studies of porcine pancreatic elastase in complex with a novel inhibitor.
- Authors
Oliveira, Tânia F; Mulchande, Jalmira; Moreira, Rui; Iley, Jim; Archer, Margarida
- 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 A. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 50.25 A, b = 57.94 A and c = 74.69 A. 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.
- Publication
Protein and peptide letters, 2007, Vol 14, Issue 1, p93
- ISSN
0929-8665
- Publication type
Journal Article
- DOI
10.2174/092986607779117173