IGF1: Difference between revisions
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Hydrophobic interaction between IGF-1 and IGFBP-4 |
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<Structure load='4xss' size='250' frame='true' align='right' caption='IGF-1/IGF-1R Complex | <Structure load='4xss' size='250' frame='true' align='right' caption='IGF-1/IGF-1R Complex' /> | ||
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hybridation of IGF1R and IR ? | hybridation of IGF1R and IR ? | ||
<Structure load='1wqj' size='250' frame='true' align='left' caption='IGF-1/IGFBP-4 Complex | <Structure load='1wqj' size='250' frame='true' align='left' caption='IGF-1/IGFBP-4 Complex' /> | ||
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The IGFBPs help to lengthen the half-life of circulating IGFs in all tissues. That is why approximately 98% of IGF-1 exists as complexed form with one of the six different IGFBP. '''IGFBP-3''', the most abundant protein, accounts for 80% of all IGF binding. Inside the liver, this mechanism is responsible for positive feedback, more precisely it allows growth hormone to continuously act upon the liver to produce more IGF-1. | The IGFBPs help to lengthen the half-life of circulating IGFs in all tissues. That is why approximately 98% of IGF-1 exists as complexed form with one of the six different IGFBP. '''IGFBP-3''', the most abundant protein, accounts for 80% of all IGF binding. Inside the liver, this mechanism is responsible for positive feedback, more precisely it allows growth hormone to continuously act upon the liver to produce more IGF-1. | ||
<scene name='75/751772/Igf-1_docking_on_igfbp/1'> | IGF-1 docks IGFBP with a series of polar and non-polar interactions all along its binding site. For instance, when IGF-1 binds IGFBP-4, <scene name='75/751772/Igf-1_docking_on_igfbp/1'>VAL48 matches PHE16</scene>. Both are hydrophobic residues. This mechanism can also be applied to all interactions between proteins of the insulin protein family such as the docking of IGF-2 in IGFBP-5. | ||
