Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin

Abstract

Cadherins are a family of Ca(2+)-dependent cell adhesion molecules containing four extracellular tandem repeats each of 110 amino acids. The most amino-terminal repeat is believed to confer the specificity of cell adhesion. A polypeptide containing the amino-terminal repeat of mouse epithelial cadherin has been over-expressed in E. coli and purified to homogeneity. This polypeptide binds Ca2+ with a dissociation constant of 1.6 x 10(-4) M. CD and NMR experiments indicate that the polypeptide adopts a predominantly beta-sheet conformation and that binding of Ca2+ induces only small conformational changes.