1H, 13C and 15N backbone assignment of the EC-1 domain of human E-cadherin

Vivitri D. Prasasty, Mary E. Krause, Usman Sumo Friend, Asokan Anbanandam, Jennifer S. Laurence, Teruna J. Siahaan

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)31-35
Number of pages5
JournalBiomolecular NMR Assignments
Issue number1
Publication statusPublished - 6 Mar 2015


  • Backbone resonance assignment
  • EC1
  • Human E-cadherin
  • Multidimensional NMR


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