Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/21516
Título: Crystallization and preliminary diffraction studies of porcine pancreatic elastase in complex with a novel inhibitor
Autor: Oliveira, Tania F.
Mulchande, Jalmira
Moreira, Rui
Iley, Jim
Archer, Margarida
Palavras-chave: Biochemistry & Molecular Biology
Data: 2007
Citação: PROTEIN AND PEPTIDE LETTERS. - Vol. 14, n. 1 (2007), p. 93-95
Resumo: 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 angstrom. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 50.25 angstrom, b = 57.94 angstrom and c = 74.69 angstrom. 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.
URI: http://hdl.handle.net/10451/21516
ISSN: 0929-8665
Aparece nas colecções:FF - Produção Científica 2000-2009

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