Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type I

被引：1
|
作者：
Unno, Masaki [1 ,2 ,3 ]
Kinjo, Saya [4 ]
Kizawa, Kenji [5 ]
Takahara, Hidenari [4 ]
机构：
[1] Ibaraki Univ, Frontier Res Ctr Appl Atom Sci, Naka, Ibaraki 3191106, Japan
[2] Ibaraki Univ, Grad Sch Sci & Engn, Hitachi, Ibaraki 3168511, Japan
[3] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
[4] Ibaraki Univ, Dept Appl Biol Resource Sci, Inashiki, Ibaraki 3000393, Japan
[5] Kanebo Cosmetics Inc, Innovat Beauty Sci Lab, Odawara, Kanagawa 2500002, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
关键词：
STRUCTURAL BASIS; HUMAN SKIN; EXPRESSION; CLONING; FAMILY; CDNA; GENE;
D O I：
10.1107/S1744309113028704
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Peptidylarginine deiminase (PAD) catalyzes the post-translational conversion of peptidylarginine to peptidylcitrulline in the presence of calcium ions. Among the five known human PAD isozymes (PAD1-4 and PAD6), PAD1 exhibits the broadest substrate specificity. Crystals of PAD1 obtained using polyethylene glycol 3350 as a precipitant diffracted to 3.70 angstrom resolution using synchrotron radiation. Two PAD1 molecules were contained in the asymmetric unit and the crystals belonged to space group P6(1), with unit-cell parameters a = b = 90.3, c = 372.3 angstrom. The solvent content was 58.2%.
引用
收藏
页码：1357 / 1359
页数：3
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