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

K I Tong; P Yau; M Overduin; S Bagby; T Porumb; M Takeichi; M Ikura

doi:10.1016/0014-5793(94)00982-1

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

FEBS Lett. 1994 Oct 3;352(3):318-22. doi: 10.1016/0014-5793(94)00982-1.

Authors

K I Tong¹, P Yau, M Overduin, S Bagby, T Porumb, M Takeichi, M Ikura

Affiliation

¹ Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.

PMID: 7925993
DOI: 10.1016/0014-5793(94)00982-1

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Cadherins / chemistry*
Cadherins / isolation & purification
Cadherins / metabolism
Calcium / metabolism
Circular Dichroism
Cloning, Molecular
Escherichia coli
Kinetics
Macromolecular Substances
Mice
Molecular Sequence Data
Peptide Fragments / chemistry*
Peptide Fragments / isolation & purification
Peptide Fragments / metabolism
Protein Binding
Protein Conformation*
Recombinant Proteins / chemistry
Recombinant Proteins / isolation & purification
Recombinant Proteins / metabolism
Restriction Mapping

Substances

Cadherins
Macromolecular Substances
Peptide Fragments
Recombinant Proteins
Calcium