TY - JOUR
T1 - Structure and properties of the C-terminal domain of insulin-like growth factor-binding protein-1 isolated from human amniotic fluid
AU - Sala, Alberto
AU - Capaldi, Stefano
AU - Campagnoli, Monica
AU - Faggion, Beniamino
AU - Labò, Sara
AU - Perduca, Massimiliano
AU - Romano, Assunta
AU - Carrizo, Maria E.
AU - Valli, Maurizia
AU - Visai, Livia
AU - Minchiotti, Lorenzo
AU - Galliano, Monica
AU - Monaco, Hugo L.
PY - 2005/8/19
Y1 - 2005/8/19
N2 - Insulin-like growth factor (IGF)-bindingprotein-1 (IG-FBP-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 Å resolution. The fragment folds as a thyroglobulin type I domain and was found to bind the Fe2+ 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.
AB - Insulin-like growth factor (IGF)-bindingprotein-1 (IG-FBP-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 Å resolution. The fragment folds as a thyroglobulin type I domain and was found to bind the Fe2+ 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.
UR - http://www.scopus.com/inward/record.url?scp=23844513418&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=23844513418&partnerID=8YFLogxK
U2 - 10.1074/jbc.M504304200
DO - 10.1074/jbc.M504304200
M3 - Article
C2 - 15972819
AN - SCOPUS:23844513418
VL - 280
SP - 29812
EP - 29819
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 33
ER -