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Horm Res. 1994;42(4-5):152-69.

The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.

Author information

1
Hagedorn Research Institute, Gentofte, Denmark.

Abstract

The nonclassical binding kinetics of IGF-I and insulin to their respective receptors, suggestive of negative cooperativity, can be readily explained by our recently proposed novel binding mechanism whereby the bivalent ligand bridges the two receptor alpha-subunits alternatively at opposite sites in a symmetrical receptor structure. The bivalent binding mechanism also explains bell-shaped bioactivity curves. The possible role of different binding modes versus differences in downstream signaling by insulin and IGF-I in producing specific mitogenic or metabolic responses is discussed.

PMID:
7868068
DOI:
10.1159/000184188
[Indexed for MEDLINE]

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