Abstract
The EC1 domain of E-cadherin has been shown to be important for cadherin-cadherin homophilic interactions. Cadherins are responsible for calcium-mediated cell-cell adhesion located at the adherens junction of the biological barriers (i.e., intestinal mucosa and the blood-brain barrier (BBB). Cadherin peptides can modulate cadherin interactions to improve drug delivery through the blood-brain barriers (BBB). However, the mechanism of modulating the E-cadherin interactions by cadherin peptides has not been fully elucidated. To provide a basis for subsequent examination of the structure and peptide-binding properties of the EC1 domain of human E-cadherin using solution NMR spectroscopy, the 1H, 13C and 15N backbone resonance of the uniformly labeled-EC1 were assigned and the secondary structure was determined based on the chemical shift values. These resonance assignments are essential for assessing protein-ligand interactions and are reported here.
Description
The final publication is available at Springer via http://dx.doi.org/10.1007/s12104-013-9539-6
Citation
Prasasty, V. D., Krause, M. E., Tambunan, U. S. F., Anbanandam, A., Laurence, J. S., & Siahaan, T. J. (2015). 1H, 13C and 15N Backbone Assignment of the EC-1 Domain of Human E-Cadherin. Biomolecular NMR Assignments, 9(1), 31–35. http://doi.org/10.1007/s12104-013-9539-6