Publicação
Crystallization and preliminary diffraction studies of porcine pancreatic elastase in complex with a novel inhibitor
| 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. |
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| Autores principais: | Oliveira, Tania F. |
| Outros Autores: | Mulchande, Jalmira; Moreira, Rui; Iley, Jim; Archer, Margarida |
| Assunto: | Biochemistry & Molecular Biology |
| Ano: | 2007 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso a metadados |
| Instituição associada: | Universidade de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório da Universidade de Lisboa |
| 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. |
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