Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex

Autor: Bradley A. Katz, Mary E. McGrath, F. R. Mistry, C. J. Linnevers, M. G. Barnes, Randall Armstrong, Dieter Brömme, James T. Palmer, J L Klaus
Rok vydání: 1997
Předmět:
Zdroj: Protein Science. 6:919-921
ISSN: 0961-8368
DOI: 10.1002/pro.5560060421
Popis: Cathepsin K is a cysteine protease of the papain family, which is predominantly expressed in osteoclasts, and is regarded as a key protease in bone remodeling. To facilitate structural studies of the protein, the wild-type sequence of the protease has been mutated so as to replace a potential N-glycosylation site. We have expressed the mutant human cathepsin K to 190 mg/5 L using the Pichia pastoris expression system. Cathepsin K was inactivated with the mechanism-based inhibitor, APC3328, and crystallized from magnesium formate. A 2.2 A X-ray data set has been collected on crystals belonging to space group P2(1)2(1)2(1), with a = 41.66 A, b = 51.41 A, and c = 107.72 A. There is most likely one molecule per asymmetric unit.
Databáze: OpenAIRE