Abstract
Cadherins are a family of Ca2+‐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 × 10−4M. CD and NMR experiments indicate that the polypeptide adopts a predominantly β‐sheet conformation and that binding of Ca2+ induces only small conformational changes.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 5:12 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 11:44 a.m.) |
Indexed | 1 year, 10 months ago (Oct. 31, 2023, 6:11 p.m.) |
Issued | 30 years, 11 months ago (Oct. 3, 1994) |
Published | 30 years, 11 months ago (Oct. 3, 1994) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 30 years, 11 months ago (Oct. 3, 1994) |
@article{I_Tong_1994, title={Purification and spectroscopic characterization of a recombinant amino‐terminal polypeptide fragment of mouse epithelial cadherin}, volume={352}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(94)00982-1}, DOI={10.1016/0014-5793(94)00982-1}, number={3}, journal={FEBS Letters}, publisher={Wiley}, author={I. Tong, Kit and Yau, Patrick and Overduin, Michael and Bagby, Stefan and Porumb, Tudor and Takeichi, Masatoshi and Ikura, Mitsuhiko}, year={1994}, month=oct, pages={318–322} }