1PBH

CRYSTAL STRUCTURE OF HUMAN RECOMBINANT PROCATHEPSIN B AT 3.2 ANGSTROM RESOLUTION

Summary for 1PBH

• Entry DOI: 10.2210/pdb1pbh/pdb
• Descriptor: PROCATHEPSIN B (1 entity in total)
• Functional Keywords: thiol protease, cathepsin b, cysteine protease, proenzyme, papain
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome: P07858
• Total number of polymer chains: 1
• Total formula weight: 35226.39

Authors

Podobnik, M.,Turk, D. (deposition date: 1997-02-14, release date: 1998-02-25, Last modification date: 2024-10-30)

Primary citation

Turk, D.,Podobnik, M.,Kuhelj, R.,Dolinar, M.,Turk, V.
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.
FEBS Lett., 384:211-214, 1996

PubMed Abstract: 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.

PubMed: 8617355
DOI: 10.1016/0014-5793(96)00309-2

Experimental method

X-RAY DIFFRACTION (3.2 Å)