Biomolecular NMR Assignments

, Volume 9, Issue 1, pp 31–35 | Cite as

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

  • Vivitri D. Prasasty
  • Mary E. Krause
  • Usman S. F. Tambunan
  • Asokan Anbanandam
  • Jennifer S. Laurence
  • Teruna J. Siahaan
Article

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.

Keywords

Human E-cadherin EC1 Backbone resonance assignment Multidimensional NMR 

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Copyright information

© Springer Science+Business Media Dordrecht 2014

Authors and Affiliations

  • Vivitri D. Prasasty
    • 1
    • 2
  • Mary E. Krause
    • 1
    • 3
  • Usman S. F. Tambunan
    • 2
  • Asokan Anbanandam
    • 4
  • Jennifer S. Laurence
    • 1
  • Teruna J. Siahaan
    • 1
  1. 1.Department of Pharmaceutical ChemistryThe University of KansasLawrenceUSA
  2. 2.Department of Chemistry, Faculty of Mathematics and Natural ScienceUniversity of IndonesiaDepokIndonesia
  3. 3.Echogen, Inc.LawrenceUSA
  4. 4.COBRE Biomolecular NMR LaboratoryThe University of KansasLawrenceUSA

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