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Article

Role of N- and C-terminal residues of insulin-like growth factor (IGF)-binding protein-3 in regulating IGF complex formation and receptor activation.

The Journal of biological chemistry - 17 Dec 2004

Yan Xiaolang, Forbes Briony E, McNeil Kerrie A, Baxter Robert C, Firth Sue M

Abstract excerpt

Insulin-like growth factor-binding protein-3 (IGFBP-3), the major IGFBP in the circulation, sequesters IGF in a stable ternary complex with the acid-labile subunit. The high affinity IGF-binding site is proposed to reside within an N-terminal hydrophobic domain in IGFBP-3, but C-terminal residues have also been implicated in the homologous protein IGFBP-5. We have mutated in various combinations Leu(77), Leu(80),...

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PMID: 15485880
DOI: 10.1074/jbc.M409345200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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