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Insulin-like growth factor II receptor as a multifunctional binding protein

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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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Author notes

  1. William J. Rutter: To whom correspondence should be addressed

Authors and Affiliations

  1. Hormone Research Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143, USA

    David O. Morgan, Jeffrey C. Edman, David N. Standring & William J. Rutter

  2. Department of Pharmacology, Stanford University School of Medicine, Stanford, California, 94305, USA

    David O. Morgan & Richard A. Roth

  3. Department of Biochemistry, St Jude Children's Hospital, 332 North Lauderdale, Memphis, Tennessee, 38105, USA

    Victor A. Fried

  4. Eli Lilly and Company, Indianapolis, Indiana, 46285, USA

    Michele C. Smith

Authors
  1. David O. Morgan
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  2. Jeffrey C. Edman
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  3. David N. Standring
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  4. Victor A. Fried
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  5. Michele C. Smith
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  6. Richard A. Roth
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  7. William J. Rutter
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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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