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1H, 13C and 15N Backbone Assignment of the EC-1 Domain of Human E-Cadherin
Prasasty, Vivitri D. Krause, Mary Elizabeth Tambunan, Usman S. F. Anbanandam, Asokan Laurence, Jennifer S. Siahaan, Teruna J.
Prasasty, Vivitri D.
Krause, Mary Elizabeth
Tambunan, Usman S. F.
Anbanandam, Asokan
Laurence, Jennifer S.
Siahaan, Teruna J.
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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.
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The final publication is available at Springer via http://dx.doi.org/10.1007/s12104-013-9539-6
Date
2014-02-08
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Springer Verlag
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Keywords
Human E-cadherin, EC1, Backbone resonance assignment, Multidimensional NMR
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