Abstract
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).
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© 1989 Plenum Press, New York
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Cascieri, M.A., Bayne, M.L. (1989). Identification of the Domains of IGF I which Interact with the IGF Receptors and Binding Proteins. In: LeRoith, D., Raizada, M.K. (eds) Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5685-1_24
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DOI: https://doi.org/10.1007/978-1-4684-5685-1_24
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