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Purification and spectroscopic characterization of a recombinant amino‐terminal polypeptide fragment of mouse epithelial cadherin
Author(s) -
I. Tong Kit,
Yau Patrick,
Overduin Michael,
Bagby Stefan,
Porumb Tudor,
Takeichi Masatoshi,
Ikura Mitsuhiko
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00982-1
Subject(s) - cadherin , amino acid , recombinant dna , tandem repeat , extracellular , cell adhesion molecule , chemistry , amino terminal , peptide sequence , biochemistry , microbiology and biotechnology , dissociation constant , cell adhesion , peptide , biology , stereochemistry , cell , gene , receptor , genome
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 −4 M. 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.