Culurgioni Simone, Muñoz Inés G, Palacios Alicia, Redondo Pilar, Blanco Francisco J, Montoya Guillermo
Structural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, Edificio 800, 48160 Derio, Spain.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):567-70. doi: 10.1107/S1744309110010080. Epub 2010 Apr 30.
Inhibitor of growth protein 4 (ING4) belongs to the ING family of tumour suppressors and is involved in chromatin remodelling, in growth arrest and, in cooperation with p53, in senescence and apoptosis. Whereas the structure and histone H3-binding properties of the C-terminal PHD domains of the ING proteins are known, no structural information is available for the N-terminal domains. This domain contains a putative oligomerization site rich in helical structure in the ING2-5 members of the family. The N-terminal domain of ING4 was overexpressed in Escherichia coli and purified to homogeneity. Crystallization experiments yielded crystals that were suitable for high-resolution X-ray diffraction analysis. The crystals belonged to the orthorhombic space group C222, with unit-cell parameters a = 129.7, b = 188.3, c = 62.7 A. The self-rotation function and the Matthews coefficient suggested the presence of three protein dimers per asymmetric unit. The crystals diffracted to a resolution of 2.3 A using synchrotron radiation at the Swiss Light Source (SLS) and the European Synchrotron Radiation Facility (ESRF).
生长抑制蛋白4（ING4）属于肿瘤抑制因子ING家族，参与染色质重塑、生长停滞，并与p53协同作用，参与衰老和凋亡过程。虽然ING蛋白C末端PHD结构域的结构和组蛋白H3结合特性已为人所知，但关于其N末端结构域尚无结构信息。该结构域在家族的ING2 - 5成员中包含一个富含螺旋结构的假定寡聚化位点。ING4的N末端结构域在大肠杆菌中过表达并纯化至同质。结晶实验得到了适合高分辨率X射线衍射分析的晶体。这些晶体属于正交晶系空间群C222，晶胞参数为a = 129.7，b = 188.3，c = 62.7 Å。自旋转函数和马修斯系数表明每个不对称单元存在三个蛋白质二聚体。使用瑞士光源（SLS）和欧洲同步辐射装置（ESRF）的同步辐射，这些晶体的衍射分辨率达到2.3 Å。
