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J. Biol. Chem., Vol. 280, Issue 33, 29812-29819, August 19, 2005

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Structure and Properties of the C-terminal Domain of Insulin-like Growth Factor-binding Protein-1 Isolated from Human Amniotic Fluid^*

Alberto Sala, Stefano Capaldi¶, Monica Campagnoli, Beniamino Faggion¶, Sara Labò, Massimiliano Perduca¶, Assunta Romano, Maria E. Carrizo¶, Maurizia Valli, Livia Visai, Lorenzo Minchiotti, Monica Galliano||, and Hugo L. Monaco¶**

From the Department of Biochemistry "A. Castellani," University of Pavia, via Taramelli 3b, 27100 Pavia, Italy and the ^¶Biocrystallography Laboratory, Department of Science and Technology, University of Verona, Ca Vignal 1, strada Le Grazie 15, 37134 Verona, Italy

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 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.

Received for publication, April 20, 2005 , and in revised form, June 21, 2005.

The atomic coordinates and structure factors (code 1ZT3 and 1ZT5) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by grants from the Italian Ministry of Education and Scientific Research (Fondo per gli Investiment della Ricerca di Base and Progetti di Ricerca di Interesse Nazionale).

Both authors contributed equally to this paper.

^|| To whom correspondence may be addressed. Tel.: 39-0382-987-724; Fax: 39-0382-423-108; E-mail: galliano{at}unipv.it.

^** To whom correspondence may be addressed. Tel.: 39-045-8027-903; Fax: 39-045-8027-929; E-mail monaco{at}sci.univr.it.

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