Please use this identifier to cite or link to this item: https://doi.org/10.1080/07391102.2012.726530
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dc.titleRemarkable disparity in mechanical response among the extracellular domains of type i and II cadherins
dc.contributor.authorLiu, R.
dc.contributor.authorWu, F.
dc.contributor.authorThiery, J.P.
dc.date.accessioned2014-11-26T10:00:09Z
dc.date.available2014-11-26T10:00:09Z
dc.date.issued2013-10-01
dc.identifier.citationLiu, R., Wu, F., Thiery, J.P. (2013-10-01). Remarkable disparity in mechanical response among the extracellular domains of type i and II cadherins. Journal of Biomolecular Structure and Dynamics 31 (10) : 1137-1149. ScholarBank@NUS Repository. https://doi.org/10.1080/07391102.2012.726530
dc.identifier.issn07391102
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/110778
dc.description.abstractCadherins, a large family of calcium-dependent adhesion molecules, are critical for intercellular adhesion. While crystallographic structures for several cadherins show clear structural similarities, their relevant adhesive strengths vary and their mechanisms of adhesion between types I and II cadherin subfamilies are still unclear. Here, stretching of cadherins was explored experimentally by atomic force microscopy and computationally by steered molecular dynamics (SMD) simulations, where partial unfolding of the E-cadherin ectodomains was observed. The SMD simulations on strand-swapping cadherin dimers displayed similarity in binding strength, suggesting contributions of other mechanisms to explain the strength differences of cell adhesion in vivo. Systematic simulations on the unfolding of the extracellular domains of type I and II cadherins revealed diverse pathways. However, at the earliest stage, a remarkable similarity in unfolding was observed for the various type I cadherins that was distinct from that for type II cadherins. This likely correlates positively with their distinct adhesive properties, suggesting that the initial forced deformation in type I cadherins may be involved in cadherin-mediated adhesion. © 2012 Taylor and Francis.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1080/07391102.2012.726530
dc.sourceScopus
dc.subjectAFM force mode
dc.subjectcalcium bridge
dc.subjectcell adhesion
dc.subjectclassical type I cadherins
dc.subjectclassical type II cadherins
dc.subjectconformational dynamics
dc.subjectE-cadherin
dc.subjectelasticity
dc.subjecthomophilic interaction
dc.subjectintermediate state
dc.subjectsingle-molecule force spectroscopy
dc.subjectSMD simulation
dc.subjectunfolding
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.contributor.departmentCANCER SCIENCE INSTITUTE OF SINGAPORE
dc.description.doi10.1080/07391102.2012.726530
dc.description.sourcetitleJournal of Biomolecular Structure and Dynamics
dc.description.volume31
dc.description.issue10
dc.description.page1137-1149
dc.description.codenJBSDD
dc.identifier.isiut000324002100010
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