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Originally published In Press as doi:10.1074/jbc.M108611200 on October 29, 2001

J. Biol. Chem., Vol. 276, Issue 52, 48930-48936, December 28, 2001
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Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure*

Simonetta BernoccoDagger §, Stéphanie Finet, Christine Ebel||, Denise EichenbergerDagger , Marlène MazzoranaDagger **, Jean FarjanelDagger , and David J. S. HulmesDagger Dagger Dagger

From the Dagger  Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard Lyon 1, 69367 Lyon cedex 7, the  European Synchrotron Radiation Facility, 38043 Grenoble cedex, and the || Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 38027 Grenoble cedex 1, France

Procollagen C-propeptide domains direct chain association during intracellular assembly of procollagen molecules. In addition, they control collagen solubility during extracellular proteolytic processing and fibril formation and interact with cell surface receptors and extracellular matrix components involved in feedback inhibition, mineralization, cell growth arrest, and chemotaxis. At present, three-dimensional structural information for the C-propeptides, which would help to understand the underlying molecular mechanisms, is lacking. Here we have carried out a biophysical study of the recombinant C-propeptide trimer from human procollagen III using laser light scattering, analytical ultracentrifugation, and small angle x-ray scattering. The results show that the trimer is an elongated molecule, which by modeling of the x-ray scattering data appears to be cruciform in shape with three large lobes and one minor lobe. We speculate that each of the major lobes corresponds to one of the three component polypeptide chains, which come together in a junction region to connect to the rest of the procollagen molecule.

* This work was supported by the Center National de la Recherche Scientifique, the Université Claude-Bernard Lyon 1, the Région Rhône-Alpes, and the Fondation pour la Recherche Médicale (a fellowship to S. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Structural Chemistry Dept., Pharmacia and Upjohn, Viale Pasteur 10, 20014 Nerviano (Milano), Italy.

** Present address: Laboratoire de Biologie Moléculaire et Cellulaire, Ecole Normale Supérieure, 69364 Lyon cedex 07, France.

Dagger Dagger To whom correspondence should be addressed: IBCP, 7 passage du Vercors, 69367 Lyon cedex 07, France. Tel.: 4-72-72-26-67; Fax: 4-72-72- 26-04; E-mail: d.hulmes@ibcp.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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