5I4H

Caught in the Act: The Crystal Structure of cleaved Cathepsin L bound to the active site of Cathepsin L

Summary for 5I4H

• Entry DOI: 10.2210/pdb5i4h/pdb
• Descriptor: Cathepsin L1, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: cathepsin, cysteine cathepsin, substrate, interaction, hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Lysosome: P07711 P07711
• Total number of polymer chains: 2
• Total formula weight: 24576.84

Authors

Sosnowski, P.,Turk, D. (deposition date: 2016-02-12, release date: 2016-04-13, Last modification date: 2024-01-10)

Primary citation

Sosnowski, P.,Turk, D.
Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.
Febs Lett., 590:1253-1261, 2016

PubMed Abstract: Cathepsin L is a ubiquitously expressed papain-like cysteine protease involved in the endosomal degradation of proteins and has numerous roles in physiological and pathological processes, such as arthritis, osteoporosis, and cancer. Insight into the specificity of cathepsin L is important for elucidating its physiological roles and drug discovery. To study interactions with synthetic ligands, we prepared a presumably inactive mutant and crystallized it. Unexpectedly, the crystal structure determined at 1.4 Å revealed that the cathepsin L molecule is cleaved, with the cleaved region trapped in the active site cleft of the neighboring molecule. Hence, the catalytic mutant demonstrated low levels of catalytic activity.

PubMed: 26992470
DOI: 10.1002/1873-3468.12140

Experimental method

X-RAY DIFFRACTION (1.42 Å)