The Type I insulin-like growth factor receptor is a physiological receptor for insulin-like growth factor II (IGF-II). To characterize the molecular basis of the receptor's ligand binding properties, we have examined the effects of alanine mutations of residues in the ligand binding site of the receptor on its affinity for IGF-II. The functional epitope for IGF-II comprises residues in the N-terminal L1 domain and residues at the C-terminus of the alpha subunit. Cysteine rich domain residues do not appear to be critical for IGF-II binding.
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