Igf1 - alec: Difference between revisions

The molecular structure of <scene name='81/814755/Igf1_structure2/2'>IGF-1</scene> tell us many things about the protein itself. Upon inspection of the structure of the IGF-1 protein side by side with <scene name='81/814755/Insulin_structure2/2'>insulin</scene>, there are three noticeable alpha helixes that are almost identical throughout the backbones of the molecules. The IGF-1 protein, being a relatively small molecule with only sixty-nine amino acids, is larger than the insulin molecule (which only has a 51 amino acid sequence). Because of the relatively small size of these molecules, they are easily transported out of the liver and pancreas into the blood and throughout the body. However, unlike insulin which is produced and stored as a hexamer containing six insulin monomers, IGF-1 is produced and stored as a monomer. Because of the structural similarities to insulin, upon the release of IGF-1 from the liver, it can bind to its own transmembrane receptors called '''<scene name='81/814755/Igf-1r/3'>IGF-1 receptors</scene>''' (IGF-1R) on cells but can also bind to the insulin receptor depending on biological conditions. Because of their structural similarities, in conditions where insulin is not present or in reduced amounts IGF-1 can bind to both insulin receptors and its own. This also works for insulin, where in conditions of low IGF-1, it can bind to both its own receptors and IGF-1R. <ref name = 'Laron'> PMID: 11577173 </ref>