Crystallization and preliminary X-ray crystallographic analysis of human autotaxin

被引：4
|
作者：
Inoue, Keigo [1 ]
Tanaka, Nobutada [1 ]
Haga, Arayo [2 ]
Yamasaki, Kyohei [1 ]
Umeda, Tomonobu [1 ]
Kusakabe, Yoshio [1 ]
Sakamoto, Yasumitsu [3 ]
Nonaka, Takamasa [3 ]
Deyashiki, Yoshihiro [4 ]
Nakamura, Kazuo T. [1 ]
机构：
[1] Showa Univ, Sch Pharm, Tokyo 1428555, Japan
[2] Gifu Pharmaceut Univ, Gifu 5028585, Japan
[3] Iwate Med Univ, Sch Pharm, Morioka, Iwate 0283694, Japan
[4] Suzuka Univ Med Sci, Fac Pharmaceut Sci, Matsusaka, Mie 5138670, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
关键词：
autotaxin; lysophosphatidic acid; lysophospholipase D; ectonucleotide pyrophosphatase; phosphodiesterase; 2; LYSOPHOSPHOLIPASE-D; PURIFICATION; MOTILITY; PROTEIN; IDENTIFICATION; ACTIVATION; SEQUENCE;
D O I：
10.1107/S174430911005311X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Autotaxin (ATX), which is also known as ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2 or ENPP2) or phosphodiesterase I alpha (PD-I alpha), is an extracellular lysophospholipase D which generates lysophosphatidic acid (LPA) from lysophosphatidylcholine (LPC). ATX stimulates tumour-cell migration, angiogenesis and metastasis and is an attractive target for cancer therapy. For crystallographic studies, the alpha isoform of human ATX was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 3.0 A resolution from a monoclinic crystal form belonging to space group C2, with unit-cell parameters a = 311.4, b = 147.9, c = 176.9 A, beta = 122.6 degrees.
引用
收藏
页码：450 / 453
页数：4
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