title: Sequence comparison and predicted structure for the four exon-encoded regions of human insulin-like growth factor binding protein 4.
abstract: The IGFBPs bind to and modulate the function of the IGFs in various ways. Human IGFBP-4 inhibits IGF mediated cell proliferation. The IGFBP exon-encoded regions were aligned and secondary structure predictions for hIGFBP-4 were developed yielding predicted 3D co-ordinates for each such region of hIGFBP-4. The exon 1 encoded region is the most conserved among the IGFBPs. That of hIGFBP-4 is predicted as an array of beta-strands that include the glycine and cysteine rich IGFBP consensus pattern and that terminate with a helix. The exon 2 encoded region is the most variable among the IGFBPs. That of hIGFBP-4 is predicted as mostly an amphipathic helix. The remaining regions are also conserved among the IGFBPs. Those of hIGFBP-4 are also predicted to contain helices. The predicted structure of hIGFBP-4 comprises amino terminal beta-strands with four helices in the carboxy terminal two thirds of the molecule.
authors.affiliation: Department of Mineral Metabolism, Pettis VA Medical Center and Loma Linda University, CA, USA.
authors.forename: E C
authors.initials: EC
authors.lastname: Landale
authors.forename: D D
authors.initials: DD
authors.lastname: Strong
authors.forename: S
authors.initials: S
authors.lastname: Mohan
authors.forename: D J
authors.initials: DJ
authors.lastname: Baylink
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D016384:Consensus Sequence / Q000235:genetics; D017124:Conserved Sequence / Q000235:genetics; D016208:Databases, Factual; D005091:Exons / Q000235:genetics*; D006801:Humans; D018974:Insulin-Like Growth Factor Binding Protein 4 / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D051381:Rats; D017386:Sequence Homology, Amino Acid
chemical_list: D018974:Insulin-Like Growth Factor Binding Protein 4