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Originally published In Press as doi:10.1074/jbc.M208956200 on October 10, 2002

J. Biol. Chem., Vol. 277, Issue 52, 50629-50635, December 27, 2002
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Mapping the Heparin-binding Site on the 13-14F3 Fragment of Fibronectin*

SachchidanandDagger , Olivier LequinDagger §, David Staunton, Barbara Mulloy||, Mark J. Forster||, Keiichi Yoshida**, and Iain D. CampbellDagger Dagger Dagger

From the Dagger  Department of Biochemistry and  Oxford Centre for Molecular Sciences, University of Oxford, South Parks Rd., Oxford OX1 3QU, United Kingdom, || National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Herts EN6 3QG, United Kingdom, and ** Mizutani Foundation for Glycoscience, 3-1-11 Nihonbashi-honcho, Chuo-ku, Tokyo 103-0023, Japan

Fibronectin, a multifunctional glycoprotein of the extracellular matrix, plays a major role in cell adhesion. Various studies have revealed that the human 13th and 14th fibronectin type III domains (labeled 13F3 and 14F3 here) contain a heparin-binding site. Mapping of the heparin-binding sites of 13-14F3, 13F3, and 14F3 by NMR chemical shift perturbation, isothermal titration calorimetry, and molecular modeling show that 13F3 provides the dominant heparin-binding site and that the residues involved are within the first 29 amino acids of 13F3. Predictions from earlier biochemical and modeling studies as well as the x-ray structure of 12-14F3 were tested. It was shown that the positively charged residues that project into the solvent from the ABE face of the triple-stranded beta  sheet on 13F3 are involved in binding, but 14F3 does not appear to contribute significantly to heparin binding.

* This work was supported by the Felix Foundation (to S.), the Federation of European Biochemical Societies (to O. L.), and the Wellcome Trust (to D. S. and I. D. C.). This is a contribution from the Oxford Centre for Molecular Sciences, which is supported by the Biotechnology and Biological Sciences Research Council, Swindon, the Medical Research Council, and The Engineering and Physical Sciences Research Council, United Kingdom.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: Laboratoire de Chimie Structurale Organique et Biologique (UMR 7613), Université Pierre et Marie Curie, Bat F74, Boite 45, 4 place Jussieu, 75252, Paris Cedex 05, France.

Dagger Dagger To whom correspondence should be addressed. Tel.: 44-1865-275990; Fax: 44-1865-275905; E-mail: idc@bioch.ox.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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