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Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin
Author(s) -
Weber Peter,
Ferber Philippe,
Fischer René,
Winterhalter Kaspar H.,
Vaughan Lloyd
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00609-6
Subject(s) - fibronectin , dermatan sulfate , heparan sulfate , heparin , chemistry , chondroitin sulfate , tenascin , binding site , glycosaminoglycan , surface plasmon resonance , binding domain , biochemistry , cell adhesion , biophysics , microbiology and biotechnology , biology , cell , materials science , nanoparticle , nanotechnology
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.