Please use this identifier to cite or link to this item:
|Title:||Molecular force spectroscopy of homophilic nectin-1 interactions|
|Authors:||Vedula, S.R.K. |
Single-molecule force spectroscopy
|Citation:||Vedula, S.R.K., Lim, T.S., Hui, S., Kausalya, P.J., Lane, E.B., Rajagopal, G., Hunziker, W., Lim, C.T. (2007-11-03). Molecular force spectroscopy of homophilic nectin-1 interactions. Biochemical and Biophysical Research Communications 362 (4) : 886-892. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2007.08.096|
|Abstract:||Nectins are Ca2+ independent cell adhesion molecules localizing at the cadherin based adherens junctions. In this study, we have used atomic force microscopy to study interaction of a chimera of extra cellular fragment of nectin-1 and Fc of human IgG (nef-1) with wild type L-fibroblasts that express endogenous nectin-1 to elucidate the biophysical characteristics of homophilic nectin-1 trans-interactions at the level of single molecule. Bond strength distribution revealed three distinct bound states (or configurations) of trans-interactions between paired nectins, where each bound state has a unique unstressed off-rate and reactive compliance. Kinetic analysis of force-dependent off-rate of the bound state involving trans-interacting V-V domains between paired nectin-1 (unstressed off-rate ∼1.465 ± 0.779 s-1, reactive compliance ∼0.143 ± 0.072 nm) was found to be closest to E-cadherin, indicating that V-V domain trans-interactions are probably necessary to initiate and promote adhesions of E-cadherin at adherens junctions (AJs). © 2007 Elsevier Inc. All rights reserved.|
|Source Title:||Biochemical and Biophysical Research Communications|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jul 13, 2018
WEB OF SCIENCETM
checked on Jun 11, 2018
checked on Jun 29, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.