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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sosnowski P,Turk Ddoi
10.1002/1873-3468.12140subject
Has Abstractpub_date
2016-04-01 00:00:00pages
1253-61issue
8eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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