Structural features of fibronectin synthetic peptide FN-C/H II, responsible for cell adhesion, neurite extension, and heparan sulfate binding.
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.
Drake
S L
SL
Department of Laboratory Medicine, University of Minnesota, Minneapolis 55455.
Varnum
J
J
Mayo
K H
KH
Letourneau
P C
PC
Furcht
L T
LT
McCarthy
J B
JB
D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion; D002642:Chick Embryo; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D006497:Heparan Sulfate / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008969:Molecular Sequence Data; D016501:Neurites; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D014407:Tumor Cells, Cultured
D005353:Fibronectins; D006497:Heparan Sulfate; D010446:Peptide Fragments; C082338:FN-C-H II peptide