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

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 cadher...

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Veröffentlicht in:FEBS letters 1994-10, Vol.352 (3), p.318-322
Hauptverfasser: I. Tong, Kit, Yau, Patrick, Overduin, Michael, Bagby, Stefan, Porumb, Tudor, Takeichi, Masatoshi, Ikura, Mitsuhiko
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Sprache:eng
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Zusammenfassung: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 Ca 2+ with a dissociation constant of 1.6 × 10 −4M. CD and NMR experiments indicate that the polypeptide adopts a predominantly β-sheet conformation and that binding of Ca 2+ induces only small conformational changes.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(94)00982-1