2pbh

Publication Abstract from PubMed

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 [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.

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.,Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V FEBS Lett. 1996 Apr 22;384(3):211-4. PMID:8617355^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.