Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin
- 8 July 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 389 (3) , 304-308
- https://doi.org/10.1016/0014-5793(96)00609-6
Abstract
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 effectKeywords
This publication has 16 references indexed in Scilit:
- Tenascins, a growing family of extracellular matrix proteinsCellular and Molecular Life Sciences, 1995
- Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R.The Journal of cell biology, 1995
- Substrate Specificity and Expression Profile of Amino Acid Transporters (AAPs) in ArabidopsisJournal of Biological Chemistry, 1995
- The Glypiated Neuronal Cell Adhesion Molecule Contactin/F11 Complexes with src-Family Protein Tyrosine Kinase FynMolecular and Cellular Neuroscience, 1995
- The tenascin gene family—versatile glycoproteins implicated in neural pattern formation and regenerationSeminars in Developmental Biology, 1995
- Tenascin-C Binds Heparin by Its Fibronectin Type III Domain FivePublished by Elsevier ,1995
- The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictinNeuron, 1993
- Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains.The Journal of cell biology, 1992
- Interactions in the Fourth DimensionBio/Technology, 1992
- Neural cell recognition molecule F11: Homology with fibronectin type III and immunoglobulin type C domainsNeuron, 1989