title: (1)H, (13)C and (15)N backbone assignment of the EC-1 domain of human E-cadherin.
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 (1)H, (13)C and (15)N 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.
authors: Department of Pharmaceutical Chemistry, The University of Kansas, Lawrence, KS, 66047, USA.
authors: Vivitri D
authors: VD
authors: Prasasty
authors: Mary E
authors: ME
authors: Krause
authors: Usman S F
authors: US
authors: Tambunan
authors: Asokan
authors: A
authors: Anbanandam
authors: Jennifer S
authors: JS
authors: Laurence
authors: Teruna J
authors: TJ
authors: Siahaan
mesh_terms: D000595:Amino Acid Sequence; D015820:Cadherins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
chemical_list: D015820:Cadherins