Production, crystallization and preliminary crystallographic analysis of an exosite-containing fragment of human von Willebrand factor-cleaving proteinase ADAMTS13

被引：5

作者：

Akiyama, Masashi ^{[1
]}

Takeda, Soichi ^{[1
]}

Kokame, Koichi ^{[1
]}

Takagi, Junichi ^{[2
]}

Miyata, Toshiyuki ^{[1
]}

机构：

[1] Natl Cardiovasc Ctr, Res Inst, Osaka 5658565, Japan

[2] Osaka Univ, Inst Prot Res, Lab Prot Synth & Express, Suita, Osaka 5650871, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷

关键词：

THROMBOTIC THROMBOCYTOPENIC PURPURA; CRYSTAL-STRUCTURES; CATALYTIC DOMAIN; CLEAVAGE; MUTATIONS; SUBSTRATE; REVEAL;

D O I：

10.1107/S1744309109023410

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom resolution, respectively.

引用

页码：739 / 742

页数：4

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