Covaceuszach S, Cattaneo A, Lamba D
Neuroscience Program and Biophysics Unit Istituto Nazionale Fisica della Materia, International School for Advanced Studies, Via Beirut 2/4, I-34014 Trieste, Italy.
Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1307-9. doi: 10.1107/s0907444901010666. Epub 2001 Aug 23.
The monoclonal antibody MNAC13 is a potent antagonist that prevents the binding of nerve-growth factor (NGF) to its tyrosine kinase A receptor (TrkA) in a variety of systems. Structural studies of the FabMNAC13 fragment were performed to gain insights into the mechanism of action of this potentially therapeutic monoclonal antibody. The optimal conditions for crystallization of FabMNAC13 were determined. Crystals appeared as prismatic bundles, displayed P2(1)2(1)2(1) space-group symmetry and diffracted to a resolution of 1.8 A. The unit-cell parameters were determined to be a = 52.73, b = 67.55, c = 111.43 A. The data set was 99.5% complete. Molecular replacement was performed, resulting in a correlation coefficient of 0.55 and an R value of 0.40. The structure refinement is now in progress.
单克隆抗体MNAC13是一种强效拮抗剂，在多种系统中可阻止神经生长因子（NGF）与其酪氨酸激酶A受体（TrkA）结合。对FabMNAC13片段进行了结构研究，以深入了解这种具有潜在治疗作用的单克隆抗体的作用机制。确定了FabMNAC13结晶的最佳条件。晶体呈棱柱束状，具有P2(1)2(1)2(1)空间群对称性，衍射分辨率达1.8 Å。确定晶胞参数为a = 52.73、b = 67.55、c = 111.43 Å。数据集完整性为99.5%。进行了分子置换，相关系数为0.55，R值为0.40。目前正在进行结构优化。
