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Title
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Production, crystallization and preliminary crystallographic analysis of an exosite-containing fragment of human von Willebrand factor-cleaving proteinase ADAMTS13.
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Authors
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M.Akiyama,
S.Takeda,
K.Kokame,
J.Takagi,
T.Miyata.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009,
65,
739-742.
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PubMed id
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Abstract
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ADAMTS13 is a reprolysin-type metalloproteinase belonging to the ADAMTS (a
disintegrin and metalloproteinase with thrombospondin type 1 motif) family. It
specifically cleaves plasma von Willebrand factor (VWF) and regulates platelet
adhesion and aggregation. ADAMTS13 is a multi-domain enzyme. In addition to the
N-terminal metalloproteinase domain, the ancillary domains, including a
disintegrin-like domain, a thrombospondin-1 type 1 repeat, a Cys-rich domain and
a spacer domain, are required for VWF recognition and cleavage. In the present
study, a fragment of the ADAMTS13 ancillary domains (ADAMTS13-DTCS; residues
287-685) was expressed using CHO Lec cells, purified and crystallized.
Diffraction data sets were collected using the SPring-8 beamline. Two
ADAMTS13-DTCS crystals with distinct unit-cell parameters generated data sets to
2.6 and 2.8 A resolution, respectively.
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