Insulin-like growth factors (IGFs: IGF1 and IGF2) are members of the insulin superfamily of hormones, which have pleiotropic roles in embryonic and postnatal growth and differentiation through activating IGF receptors (IGFRs: IGF1R and IGF2R) and the insulin receptor signaling cascade. In the circulation, IGFs can form binary complexes (10%–15%) with IGF-binding proteins (IGFBPs: IGFBP1, IGFBP2, IGFBP4, or IGFBP6), or ternary complexes (80%–90%) with IGFBPs (IGFBP3 or IGFBP5) and acid-labile subunit (ALS). Free IGFs in serum have a half-life of less than 10 min, but a binary complex increases this half-life to 30–90 min, whereas a ternary complex maintains it up to 16–24 h. These imply that the binary (IGF/IGFBP) and ternary complexes (IGF/IGFBP/ALS) transport IGFs, protect them from degradation for a prolonged half-life, and limit their binding to IGFRs. Here you can see the structure of Human IGF1/IGFBP3/ALS Ternary Complex determined by cryoEM (PDB code: 7WRQ)
#molecularart ... #immolecular ... #insulin-like ... #hormone ... #complex .. #stability ... #degradation ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #insulin-like ... #hormone ... #complex .. #stability ... #degradation ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
