Direct molecular force measurements of multiple adhesive interactions between cadherin ectodomains Journal Article


Authors: Sivasankar, S.; Brieher, W.; Lavrik, N.; Gumbiner, B.; Leckband, D.
Article Title: Direct molecular force measurements of multiple adhesive interactions between cadherin ectodomains
Abstract: Direct-force measurements of the interactions between recombinant C- cadherin from Xenopus demonstrated that the ectodomain of cadherin exhibits multiple adhesive contacts that involve successive domains along the extracellular region of the protein. Contacts between the fully interdigitated antiparallel proteins form the strongest adhesive interaction. A second weaker minimum was measured when the interdigitated proteins were separated by a distance equal to the length of one domain of the extracellular (EC) fragment and corresponding to the antiparallel alignment of domains one through four (EC1 through EC4). The successive rupture of these interactions generates an unbinding force profile that may be optimized to impede the abrupt failure of cadherin-mediated junctions under force.
Keywords: controlled study; nonhuman; protein domain; protein interaction; recombinant protein; measurement; molecular interaction; cadherin; xenopus; force; adhesion; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 96
Issue: 21
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1999-10-12
Start Page: 11820
End Page: 11824
Language: English
DOI: 10.1073/pnas.96.21.11820
PROVIDER: scopus
PMCID: PMC18370
PUBMED: 10518534
DOI/URL:
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
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  1. William M Brieher
    14 Brieher