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Protein Science, Vol 6, Issue 4 919-921, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

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

C. J. LINNEVERS, M. E. MCGRATH, R. ARMSTRONG, F. R. MISTRY, M. G. BARNES, J. L. KLAUS, J. T. PALMER, B. A. KATZ and D. BROMME
Arris Pharmaceutical, 385 Oyster Point Blvd., Suite 3, South San Francisco, California 94080

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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