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J Biol Chem. 2002 Dec 27;277(52):50629-35. Epub 2002 Oct 10.

Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin.

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  • 1Department of Biochemistry and Oxford Centre for Molecular Sciences, University of Oxford, South Parks Rd., Oxford OX1 3QU, United Kingdom.

Abstract

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 (13)F3 and (14)F3 here) contain a heparin-binding site. Mapping of the heparin-binding sites of (13-14)F3, (13)F3, and (14)F3 by NMR chemical shift perturbation, isothermal titration calorimetry, and molecular modeling show that (13)F3 provides the dominant heparin-binding site and that the residues involved are within the first 29 amino acids of (13)F3. Predictions from earlier biochemical and modeling studies as well as the x-ray structure of (12-14)F3 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 (13)F3 are involved in binding, but (14)F3 does not appear to contribute significantly to heparin binding.

PMID:
12377765
[PubMed - indexed for MEDLINE]
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