Author/Editor		Štern, Igor
Title		Določanje tridemnzionalne strukture kompleksov katepsinov s sintetičnimi inhibitorji
Type		monografija
Place		Ljubljana
Publisher		Medicinska fakulteta
Publication year		2001
Volume		str. 46
Language		slo
Abstract		Low molecular weight synthetic inhibitors are tools for studies of the physiological role of enzymes. Determination of the crystal structure of NS-134, a cathepsin B inhibitor, in complex with the bovine cathepsin B is part of development of double-head epoxisuccinyl based inhibitors of lysosomal cysteine proteases. The structure has confirmed the correctness of modeling of the structure of binding geometry of novel inhibitors on the basis of known crystal structures of the complexes of inhibitors bound into the active site cleft of lysosomal cysteine proteases. The structure interpretation revealed that selectivity and affinity of binding of these inhibitors are not additive factors and that design of a successful inhibitor is actually a compromise taking into account both factors.
Descriptors		CATHEPSIN B CYSTEINE PROTEINASE INHIBITORS PROTEIN CONFORMATION BINDING SITES PROTEIN BINDING