人类EF手型肿瘤抑制蛋白S100A2的纯化与结晶
Purification and crystallization of the human EF-hand tumour suppressor protein S100A2.
作者信息
Koch Michael, Diez Joachim, Fritz Günter
机构信息
Fachbereich Biologie, Universität Konstanz, Postfach M665, Universitätsstrasse 10, 78457 Konstanz, Germany.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1120-3. doi: 10.1107/S1744309106039881. Epub 2006 Oct 20.
S100A2 is a Ca(2+)-binding EF-hand protein that is mainly localized in the nucleus. There, it acts as a tumour suppressor by binding and activating p53. Wild-type S100A2 and a S100A2 variant lacking cysteines have been purified. CD spectroscopy showed that there are no changes in secondary-structure composition. The S100A2 mutant was crystallized in a calcium-free form. The crystals, with dimensions 30 x 30 x 70 microm, diffract to 1.7 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 43.5, b = 57.8, c = 59.8 A, alpha = beta = gamma = 90 degrees. Preliminary analysis of the X-ray data indicates that there are two subunits per asymmetric unit.
S100A2是一种结合钙的EF手型蛋白，主要定位于细胞核。在细胞核中，它通过结合并激活p53发挥肿瘤抑制作用。野生型S100A2和一种不含半胱氨酸的S100A2变体已被纯化。圆二色光谱显示二级结构组成没有变化。S100A2突变体以无钙形式结晶。晶体尺寸为30×30×70微米，衍射分辨率为1.7埃，属于空间群P2(1)2(1)2(1)，晶胞参数a = 43.5，b = 57.8，c = 59.8埃，α = β = γ = 90°。对X射线数据的初步分析表明，每个不对称单元有两个亚基。
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