Abstract
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.
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Morgan, D., Edman, J., Standring, D. et al. Insulin-like growth factor II receptor as a multifunctional binding protein. Nature 329, 301–307 (1987). https://doi.org/10.1038/329301a0
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DOI: https://doi.org/10.1038/329301a0
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