Unno Masaki, Kinjo Saya, Kizawa Kenji, Takahara Hidenari
Frontier Research Center for Applied Atomic Sciences, Ibaraki University, 162-1 Shirakata, Tokai, Naka, Ibaraki 319-1106, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1357-9. doi: 10.1107/S1744309113028704. Epub 2013 Nov 28.
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 Å 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 Å. The solvent content was 58.2%.
肽基精氨酸脱亚氨酶（PAD）在钙离子存在的情况下催化肽基精氨酸的翻译后转化为肽基瓜氨酸。在五种已知的人类PAD同工酶（PAD1 - 4和PAD6）中，PAD1表现出最广泛的底物特异性。使用聚乙二醇3350作为沉淀剂获得的PAD1晶体，利用同步辐射衍射至3.70 Å分辨率。不对称单元中包含两个PAD1分子，晶体属于空间群P6(1)，晶胞参数a = b = 90.3，c = 372.3 Å。溶剂含量为58.2%。
