1H, 13C and 15N Backbone Assignment of the EC-1 Domain of Human E-Cadherin

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Issue Date
2014-02-08Author
Prasasty, Vivitri D.
Krause, Mary Elizabeth
Tambunan, Usman S. F.
Anbanandam, Asokan
Laurence, Jennifer S.
Siahaan, Teruna J.
Publisher
Springer Verlag
Type
Article
Article Version
Scholarly/refereed, author accepted manuscript
Rights
© Springer Science+Business Media Dordrecht 2014
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Show full item recordAbstract
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
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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
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