Morgan D O, Edman J C, Standring D N, Fried V A, Smith M C, Roth R A, Rutter W J
Nature. 1987;329(6137):301-7. doi: 10.1038/329301a0.
The primary structure of human insulin-like growth factor II receptor, predicted from the complementary DNA sequence, reveals a transmembrane receptor molecule with a large extracellular domain made up of fifteen repeat sequences and a small region homologous to the collagen-binding domain of fibronectin. The structural and biochemical features of the IGF-II receptor appear identical to those of the cation-independent mannose-6-phosphate receptor.
从互补DNA序列预测的人胰岛素样生长因子II受体的一级结构,揭示了一种跨膜受体分子,其具有由15个重复序列组成的大的细胞外结构域和与纤连蛋白的胶原结合结构域同源的小区域。IGF-II受体的结构和生化特征似乎与不依赖阳离子的甘露糖-6-磷酸受体的结构和生化特征相同。