Avtor/Urednik		Štern, Igor
Naslov		Določanje tridemnzionalne strukture kompleksov katepsinov s sintetičnimi inhibitorji
Tip		monografija
Kraj izdaje		Ljubljana
Založnik		Medicinska fakulteta
Leto izdaje		2001
Obseg		str. 46
Jezik		slo
Abstrakt		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.
Deskriptorji		CATHEPSIN B CYSTEINE PROTEINASE INHIBITORS PROTEIN CONFORMATION BINDING SITES PROTEIN BINDING