Sequence-specific resonance assignments and partial unfolding of extracellular domains II and III of E-cadherin.

Epithelial cadherin (E-cadherin) is a transmembrane receptor that plays a vital role in Ca2+-dependent homotypic cell–cell adhesion processes (Takeichi, 1991). The extracellular domain of E-cadherin contains five tandem repeats of about 100 amino acid residues, and is responsible for recognizing cadherin molecules of the same type in a calcium-dependent manner (for a review, see Alattia et al., 1999). The determination of the three-dimensional structure and dynamics of the cadherin extracellular domain in the presence and in the absence of Ca2+ should help us understand how cadherin interacts with Ca2+ ions and mediates cell adhesion functions.