1ZT3

C-terminal domain of Insulin-like Growth Factor Binding Protein-1 isolated from human amniotic fluid

Summary for 1ZT3

• Entry DOI: 10.2210/pdb1zt3/pdb
• Related: 1ZT5
• Descriptor: Insulin-like growth factor binding protein 1, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
• Functional Keywords: insulin-like growth factor binding protein-1, igfbp-1, amniotic fluid, c-terminal domain, metal-binding, peptide binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P08833
• Total number of polymer chains: 1
• Total formula weight: 9273.44

Authors

Sala, A.,Capaldi, S.,Campagnoli, M.,Faggion, B.,Labo, S.,Perduca, M.,Romano, A.,Carrizo, M.E.,Valli, M.,Visai, L.,Minchiotti, L.,Galliano, M.,Monaco, H.L. (deposition date: 2005-05-26, release date: 2005-06-28, Last modification date: 2024-10-16)

Primary citation

Sala, A.,Capaldi, S.,Campagnoli, M.,Faggion, B.,Labo, S.,Perduca, M.,Romano, A.,Carrizo, M.E.,Valli, M.,Visai, L.,Minchiotti, L.,Galliano, M.,Monaco, H.L.
Structure and Properties of the C-terminal Domain of Insulin-like Growth Factor-binding Protein-1 Isolated from Human Amniotic Fluid
J.Biol.Chem., 280:29812-29819, 2005

PubMed Abstract: Insulin-like growth factor (IGF)-binding protein-1 (IGFBP-1) regulates the activity of the insulin-like growth factors in early pregnancy and is, thus, thought to play a key role at the fetal-maternal interface. The C-terminal domain of IGFBP-1 and three isoforms of the intact protein were isolated from human amniotic fluid, and sequencing of the four N-terminal polypeptide chains showed them to be highly pure. The addition of both intact IGFBP-1 and its C-terminal fragment to cultured fibroblasts has a similar stimulating effect on cell migration, and therefore, the domain has a biological activity on its own. The three-dimensional structure of the C-terminal domain was determined by x-ray crystallography to 1.8 Angstroms resolution. The fragment folds as a thyroglobulin type I domain and was found to bind the Fe(2+) ion in the crystals through the only histidine residue present in the polypeptide chain. Iron (II) decreases the binding of intact IGFBP-1 and the C-terminal domain to IGF-II, suggesting that the metal binding site is close to or part of the surface of interaction of the two molecules.

PubMed: 15972819
DOI: 10.1074/jbc.M504304200

Experimental method

X-RAY DIFFRACTION (1.8 Å)