Structural features of fibronectin synthetic peptide FN-C/H II, responsible for cell adhesion, neurite extension, and heparan sulfate binding

S. L. Drake, J. Varnum, K. H. Mayo, P. C. Letourneau, L. T. Furcht, J. B. McCarthy

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

FN-C/H II (KNNQKSEPLIGRKKT), a heparin-binding peptide derived from the COOH-terminal heparin-binding domain of fibronectin, mediates cell adhesion for a variety of cell types and promotes neurite outgrowth. By systematic amino acid substitution of synthetic peptide analogues of FN-C/H II, the basic structural features necessary for activity have been identified in the COOH-terminal residues LIGRKK. This biologically 'active' sequence has been located in several other heparin/heparan sulfate-binding proteins and may represent a potential binding motif for sulfated polyanions. NMR structural studies indicate that the COOH-terminal segment of FN-C/H II displays significant multiple-turn or helix-like character suggesting that the RKK sequence may lie on the same surface of the protein, as opposed to alternating in an extended chain motif.

Original languageEnglish (US)
Pages (from-to)15859-15867
Number of pages9
JournalJournal of Biological Chemistry
Volume268
Issue number21
StatePublished - 1993

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