Avtor/Urednik		Turk, D; Podobnik, M; Kuhelj, R; Dolinar, M; Turk, V
Naslov		Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
Tip		članek
Vir		FEBS Lett
Vol. in št.		Letnik 384, št. 3
Leto izdaje		1996
Obseg		str. 211-4
Jezik		eng
Abstrakt		A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme ŠMusil et al. (1991) EMBO J. 10, 2321-2330Ć: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.
Deskriptorji		CATHEPSIN B CRYSTALLOGRAPHY, X-RAY ENZYME PRECURSORS BINDING SITES CYSTEINE PROTEINASES MODELS, MOLECULAR PAPAIN PEPTIDE FRAGMENTS PROTEIN CONFORMATION STRUCTURE-ACTIVITY RELATIONSHIP