Majeti R, Bilwes A M, Noel J P, Hunter T, Weiss A
Department of Microbiology, University of California, San Francisco, CA 94143, USA.
Science. 1998 Jan 2;279(5347):88-91. doi: 10.1126/science.279.5347.88.
The function and regulation of the receptorlike transmembrane protein tyrosine phosphatases (RPTPs) are not well understood. Ligand-induced dimerization inhibited the function of the epidermal growth factor receptor (EGFR)-RPTP CD45 chimera (EGFR-CD45) in T cell signal transduction. Properties of mutated EGFR-CD45 chimeras supported a general model for the regulation of RPTPs, derived from the crystal structure of the RPTPalpha membrane-proximal phosphatase domain. The phosphatase domain apparently forms a symmetrical dimer in which the catalytic site of one molecule is blocked by specific contacts with a wedge from the other.
类受体跨膜蛋白酪氨酸磷酸酶（RPTPs）的功能及调控机制尚未完全明确。在T细胞信号转导过程中，配体诱导的二聚化作用会抑制表皮生长因子受体（EGFR）-RPTP CD45嵌合体（EGFR-CD45）的功能。突变型EGFR-CD45嵌合体的特性支持了一种基于RPTPalpha膜近端磷酸酶结构域晶体结构推导出来的RPTPs调控通用模型。磷酸酶结构域显然形成了一个对称二聚体，其中一个分子的催化位点被来自另一个分子的楔形结构的特定接触所阻断。
