Insulin-like growth factor binding proteins (IGFBPs) control bioavailability, activity and distribution of IGF-1 and -2 through high-affinity IGFBP-IGF complexes. To analyze the interactions of N- and C-terminal domain of IGFBPs with IGF-1, the several X-ray structures of IGFBP-IGF complexes were determind. These crystal structures provide the molecular basis for the IGFBPs regulation of IGF signaling and support research into the design of IGFBP variants as therapeutic IGF inhibitors for diseases of IGF disregulation.
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Insulin-like growth factor binding proteins (IGFBPs) control bioavailability, activity and distribution of IGF-1 and -2 through high-affinity IGFBP-IGF complexes. To analyze the interactions of N- and C-terminal domain of IGFBPs with IGF-1, the several X-ray structures of IGFBP-IGF complexes were determind. These crystal structures provide the molecular basis for the IGFBPs regulation of IGF signaling and support research into the design of IGFBP variants as therapeutic IGF inhibitors for diseas...
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