Abstract
The Extracellular 1 (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 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.
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Acknowledgments
This work is supported by a grant from NIH/NINDS (R01 NS075374-01). M.E.K. was supported by a PhRMA Foundation Postdoctoral Fellowship in Pharmaceutics. The authors would like to thank to the NMR Facility of the NIH COBRE Protein Structure and Function Grant (P20 RR017708).
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Prasasty, V.D., Krause, M.E., Tambunan, U.S.F. et al. 1H, 13C and 15N backbone assignment of the EC-1 domain of human E-cadherin. Biomol NMR Assign 9, 31–35 (2015). https://doi.org/10.1007/s12104-013-9539-6
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DOI: https://doi.org/10.1007/s12104-013-9539-6