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Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors.
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.
PMID: 6189745 [PubMed - indexed for MEDLINE]
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Cited by 12 PubMed Central articles
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Insulin capture by an insulin-linked polymorphic region G-quadruplex DNA oligonucleotide.
Connor AC, Frederick KA, Morgan EJ, McGown LB.
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[J Am Chem Soc. 2006]
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Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins.
Terasawa H, Kohda D, Hatanaka H, Nagata K, Higashihashi N, Fujiwara H, Sakano K, Inagaki F.
EMBO J. 1994 Dec 1; 13(23):5590-7.
[EMBO J. 1994]
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Purification and partial sequence analysis of insulin-like growth factor-1 from bovine colostrum.
Francis GL, Read LC, Ballard FJ, Bagley CJ, Upton FM, Gravestock PM, Wallace JC.
Biochem J. 1986 Jan 1; 233(1):207-13.
[Biochem J. 1986]
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