STRUCTURAL STUDIES OF RECEPTOR SIGNALING CRYSTAL STRUCTURES

配体结合域的晶体结构 神经营养因子受体TrkA、TrkB和TrkC已被解决，并 使用在SSRL收集的同步加速器数据进行精炼。这些蛋白质是 折叠错误，但一个琐碎的建模操作就会产生正确的 拓扑学。派生结构确认唯一的 表面上的二硫化物，并允许讨论丙氨酸扫描数据 和配基结合决定因素。这将有助于研究 神经生长因子。

The crystal structures of the ligand binding domains of the neurotrophin receptors trkA, trkB, and trkC have been solved and refined using synchrotron data collected at SSRL. The proteins are mis-folded, but a trivial modeling exercise produces the correct topology. The derived structures confirm the placement of a unique disulfide on the surface and allow discussion of Alanine-scanning data and ligand binding determinants. This will facilitate research into neuronal growth factors.