Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1698, Issue 2, Pages 255-259Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2003.11.035
Keywords
crystal; aspartyl protease; soluble enzyme; beta-secretase; glycosylation; autoprocessing
Categories
Ask authors/readers for more resources
Human p-amyloid precursor protein cleaving enzyme (beta-secretase, or BACE) belongs to the aspartyl protease family, and is responsible for generating the N-terminus of beta-amyloid peptide (Abeta). BACE is a type I transmembrane glycoprotein with pre-, pro- and catalytic domains, a short transmembrane helix and a cytoplasmic region. In this study, a truncated form was engineered to produce the authentic catalytic domain of BACE in Trichoplusia ni (High 5(TM)) cells. The glycosylated BACE zymogen (proBACE) was secreted into the conditioned medium for facile purification by metal chelate and gel filtration chromatographies. The mature catalytic domain was obtained by a trans cleavage event under acidic conditions and crystallized in the absence of a bound inhibitor. A complete 3.4 Angstrom data set was collected on a single orthorhombic crystal with unit cell parameters a = 74 Angstrom, b = 130 Angstrom, c = 134 Angstrom. Successful molecular replacement shows two BACE molecules in the asymmetric unit. (C) 2004 Published by Elsevier B.V.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available