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. 1997 Apr;6(4):919–921. doi: 10.1002/pro.5560060421

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

C J Linnevers 1, M E McGrath 1, R Armstrong 1, F R Mistry 1, M G Barnes 1, J L Klaus 1, J T Palmer 1, B A Katz 1, D Brömme 1
PMCID: PMC2144758  PMID: 9098904

Abstract

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.

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Selected References

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