Mazlo J, Stanfield R L, Wilson I A, Hinrichs S H, Stezowski J J
Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):462-4. doi: 10.1107/s0907444901001135.
The binding of transcription factor ATF-1 to DNA contributes to gene expression and regulation of cell growth. Antibody Mab41.4, raised against ATF-1, and its derivatives Fab41.4 and scFv41.4 inhibit specific DNA binding in vitro and induce apoptotic death of tumor cells in vivo. Structural studies of Fab41.4 were performed to gain insight into the mechanism of action of this potentially therapeutic antibody. The optimal conditions for crystallization of Fab41.4 were determined. Crystals were needle-like in appearance, displayed C2 space-group symmetry and diffracted to a resolution of 1.6 A. The unit-cell parameters were determined to be a = 186.64, b = 40.22, c = 55.58 A, alpha = gamma = 90, beta = 96.93 degrees. The data set was 97.7% complete. Molecular replacement was performed, resulting in an R value of 44.6%.
转录因子ATF-1与DNA的结合有助于基因表达和细胞生长的调控。针对ATF-1产生的单克隆抗体Mab41.4及其衍生物Fab41.4和单链抗体scFv41.4在体外可抑制特异性DNA结合，并在体内诱导肿瘤细胞凋亡死亡。对Fab41.4进行结构研究以深入了解这种潜在治疗性抗体的作用机制。确定了Fab41.4结晶的最佳条件。晶体外观呈针状，具有C2空间群对称性，衍射分辨率为1.6 Å。晶胞参数确定为a = 186.64，b = 40.22，c = 55.58 Å，α = γ = 90，β = 96.93°。数据集完整性为97.7%。进行了分子置换，得到的R值为44.6%。
