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E-cadherin is a transmembrane protein that provides Ca²⁺-dependent cell adhesion to epithelial cells. The large majority of the ¹H, ¹⁵N, ¹³C and ¹³CO resonances of a 146-amino acid polypeptide from epithelial (E-) cadherin have been assigned using multidimensional NMR spectroscopy. The structure of the amino-terminal 100 amino acids, corresponding to the first extracellular repeat of E-cadherin [Overduin et al. (1995) Science, 267, 386–389], has been refined. The monomeric state of this isolated domain is demonstrated by light scattering and sedimentation analysis. Seven β-strands and two short helices were identified by patterns of NOE cross-peaks, vicinal coupling constants and chemical shift indices. A novel structural motif termed a quasi-β-helix found in the crystal structure of a neural (N-) cadherin domain [Shapiro et al. (1995) Nature, 374, 327–337] is characterized in detail for the first time …