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Posttranslational Modification of the IGF Binding Proteins

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Book cover The IGF System

Part of the book series: Contemporary Endocrinology ((COE,volume 17))

Abstract

Primary sequences for the six currently characterized insulin-like growth factor binding proteins (IGFBPs) range in length from 201 amino acids for rat IGFBP-6 to 289 amino acids for human IGFBP-2 (1). Sequence analyses indicate extensive homology among the IGFBPs in the amino(N)- and carboxy(C)-terminal domains with their conserved cysteines, domains that confer the ability to bind IGF ligand with high affinity. The homology within the IGF-binding end portions of the molecule defines the family of IGFBPs. However, it is the unique central domain that makes each IGFBP structurally and ultimately functionally distinctive.

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Conover, C.A. (1999). Posttranslational Modification of the IGF Binding Proteins. In: Rosenfeld, R.G., Roberts, C.T. (eds) The IGF System. Contemporary Endocrinology, vol 17. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-712-3_16

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