Cooperativity of the N- and C-terminal domains of insulin-like growth factor (IGF) binding protein 2 in IGF binding

The cross-linking and nuclear magnetic resonance (NMR) spectroscopy was used to study the molecular interactions among the N-domain of insulin-like growth factor-binding protein-2 (IGFBP-2) (N-BP-2), C-BP-2, and IGFs. The results reveal that low molecular weight heparin bound to the IGF-I*N-BP-2*C-BP-2 ternary complex but did not cause it to dissociate.