Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin.
The structural basis for the interaction between tenascin-C and the neuronal cell adhesion molecule, contactin/F11, was investigated using plasmon surface resonance technology. The binding site on tenascin-C for contactin/F11 is shown to span the two fibronectin type III homology domains 5 and 6. Either domain alone is insufficient for binding. Heparin, heparan sulfate and dermatan sulfate inhibit this interaction through binding to a conserved heparin-binding site on domain 5. In contrast, chondroitin sulfates A and C have no such effect.
Weber
P
P
Laboratorium für Biochemie I, Zürich, Switzerland.
Ferber
P
P
Fischer
R
R
Winterhalter
K H
KH
Vaughan
L
L
D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D015816:Cell Adhesion Molecules, Neuronal; D002642:Chick Embryo; D058966:Contactins; D003871:Dermatan Sulfate / Q000494:pharmacology; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000494:pharmacology; D006493:Heparin / Q000494:pharmacology*; D006497:Heparan Sulfate / Q000494:pharmacology; D008562:Membrane Glycoproteins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D019006:Neural Cell Adhesion Molecules / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D019063:Tenascin / Q000737:chemistry / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D015816:Cell Adhesion Molecules, Neuronal; D058966:Contactins; D003871:Dermatan Sulfate; D005353:Fibronectins; D006025:Glycosaminoglycans; D006493:Heparin; D006497:Heparan Sulfate; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D019006:Neural Cell Adhesion Molecules; D011993:Recombinant Fusion Proteins; D019063:Tenascin