Molecular bases for human leucocyte elastase inhibition.
Human leucocyte elastase is a serine proteinase involved in phagocytosis, defence against invading micro-organisms, degradation of elastin, collagen, proteoglycans, fibrinogen and fibrin, being also responsible for the digestion of damaged tissues and of the bacterial degradation products. Lack of the enzyme regulation is at the basis of pathological states, such as pulmonary emphysema, cystic fibrosis, rheumatoid arthritis, atherosclerosis and glomerulonephritis. A detailed characterisation of the enzyme:inhibitor recognition process, based on extensive thermodynamic, kinetic and structural information, as well as on the comparative analysis with the homologous proteinase from porcine pancreas, is reported in the present review.
Bolognesi
M
M
Dipartimento di Genetica e Microbiologia, Università di Pavia, Italy.
Djinović-Carugo
K
K
Ascenzi
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003196:Computer Graphics; D006801:Humans; D007962:Leukocytes / Q000201:enzymology*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010059:Ovomucin / Q000037:antagonists & inhibitors* / Q000378:metabolism; D010196:Pancreatic Elastase / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding; D011487:Protein Conformation; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*
D015842:Serine Proteinase Inhibitors; D010059:Ovomucin; D010196:Pancreatic Elastase