Crystallization and preliminary diffraction studies of porcine pancreatic elastase in complex with a novel inhibitor.
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.
Oliveira
Tânia F
TF
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, ITQB-UNL, Av. República, Apt. 127, 2781-901 Oeiras, Portugal.
Mulchande
Jalmira
J
Moreira
Rui
R
Iley
Jim
J
Archer
Margarida
M
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D008958:Models, Molecular; D015394:Molecular Structure; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000302:isolation & purification; D013552:Swine
D004791:Enzyme Inhibitors; D010196:Pancreatic Elastase