Format

Send to

Choose Destination
See comment in PubMed Commons below
Arch Biochem Biophys. 2002 Apr 1;400(1):141-7.

Both the dimerization and immunochemical properties of E-cadherin EC1 domain depend on Trp(156) residue.

Author information

1
Division of Dermatology, Washington University Medical School, St. Louis, Missouri 63110, USA.

Abstract

Using site-directed mutagenesis, we show in this paper that the adhesive interface detected in cadherin crystals is unlikely to mediate adhesive interaction between myc- and flag-tagged E-cadherin molecules in human A-431 cells. We also found that a critical residue within this interface, His(233), is part of the epitope for mAb SHE78-7. This epitope was accessible to the antibody in the adhesive E-cadherin dimers, which is consistent with uninvolvement of the site containing His(233) in cell-cell adhesion. However, both the adhesive dimerization and the integrity of the SHE78-7 epitope depended on the same intramolecular interaction between Trp(156) and its hydrophobic pocket. Our data suggest that this interaction may have an important regulatory function in controlling the surface topology of the NH(2)-terminal domain of E-cadherin.

PMID:
11913981
DOI:
10.1006/abbi.2002.2774
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center