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 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(94)00982-1 |