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      The Insulin-Like Growth Factor-I Receptor

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          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 α-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.

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          Author and article information

          Journal
          Hormone Research
          Horm Res
          S. Karger AG
          1423-0046
          0301-0163
          1994
          1994
          : 42
          : 4-5
          : 152-169
          Article
          10.1159/000184188
          © 1994
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