Three-dimensional models for human insulinlike growth factors (IGF-I and IGF-II) have been constructed by using interactive molecular graphics. It is suggested that the two growth factors have structures in which the A and B chains and the hydrophobic cores are identical to those of insulin. The conformations of the connecting peptides and COOH-terminal extensions are predicted by statistical methods but the structures are limited by the constraints implied by the insulinlike part. The models explain the nonsuppressibility by anti-insulin antibodies of the IGFs and show that part of the insulin receptor-binding region is conserved, which explains the growth factors' ability to bind insulin receptors.
Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors.,Blundell TL, Bedarkar S, Humbel RE Fed Proc. 1983 Jun;42(9):2592-7. PMID:6189745
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Blundell TL, Bedarkar S, Humbel RE. Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors. Fed Proc. 1983 Jun;42(9):2592-7. PMID:6189745