Identification of the Domains of IGF I which Interact with the IGF Receptors and Binding Proteins

  • Margaret A. Cascieri
  • Marvin L. Bayne


The elucidation of the primary sequence of human insulin-like growth factor I (IGF I) (1) and the subsequent modeling of its secondary and tertiary structure based on its homology with insulin (2,3) have made it possible to predict which structural features of this peptide are involved in its binding to the types 1 and 2 IGF receptors and to soluble IGF binding proteins. The amino terminal 29 amino acids of IGF I (B-region) are homologous with the B-chain of insulin. A 12 amino acid linking sequence (C-region) joins the B-region with a 21 amino acid A-region which is homologous to the A-chain of insulin. The molecule terminates with an 8 amino acid sequence termed the D-region (Figure 1).


Insulin Receptor Aromatic Residue Serum Binding Protein Normal Affinity Reduce Binding Affinity 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Margaret A. Cascieri
    • 1
  • Marvin L. Bayne
    • 1
  1. 1.Departments of Biochemical Endocrinology and Growth Factor ResearchMerck Sharp & Dohme Research LaboratoriesRahwayUSA

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