Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jsb.2014.01.001
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dc.titleA site for direct integrin αvβ6·uPAR interaction from structural modelling and docking
dc.contributor.authorSowmya, G.
dc.contributor.authorKhan, J.M.
dc.contributor.authorAnand, S.
dc.contributor.authorAhn, S.B.
dc.contributor.authorBaker, M.S.
dc.contributor.authorRanganathan, S.
dc.date.accessioned2014-11-26T07:42:27Z
dc.date.available2014-11-26T07:42:27Z
dc.date.issued2014-03
dc.identifier.citationSowmya, G., Khan, J.M., Anand, S., Ahn, S.B., Baker, M.S., Ranganathan, S. (2014-03). A site for direct integrin αvβ6·uPAR interaction from structural modelling and docking. Journal of Structural Biology 185 (3) : 327-335. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jsb.2014.01.001
dc.identifier.issn10478477
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/109150
dc.description.abstractIntegrin αvβ6 is an epithelially-restricted heterodimeric transmembrane glycoprotein, known to interact with the urokinase plasminogen activating receptor (uPAR), playing a critical role in cancer progression. While the X-ray crystallographic structures of segments of other integrin heterodimers are known, there is no structural information for the complete αvβ6 integrin to assess its direct interaction with uPAR. We have performed structural analysis of αvβ6·uPAR interactions using model data with docking simulations to pinpoint their interface, in accord with earlier reports of the β-propeller region of integrin α-chain interacting with uPAR. Interaction of αvβ6·uPAR was demonstrated by our previous study using immunoprecipitation coupled with proteomic analysis by mass spectrometry. Recently this interaction was validated with proximity ligation assays and peptide arrays. The data suggested that two potential peptide regions from domain II and one peptide region from domain III of uPAR, interact with αvβ6 integrin. Only the peptide region from domain III is consistent with the three-dimensional interaction site proposed in this study. The molecular basis of integrin αvβ6·uPAR binding using structural data is discussed for its implications as a potential therapeutic target in cancer management. © 2014 Elsevier Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jsb.2014.01.001
dc.sourceScopus
dc.subjectIntegrin αvβ6
dc.subjectIntegrin heterodimer
dc.subjectMolecular docking
dc.subjectProtein-protein interactions
dc.subjectStructural modelling
dc.subjectUPAR
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/j.jsb.2014.01.001
dc.description.sourcetitleJournal of Structural Biology
dc.description.volume185
dc.description.issue3
dc.description.page327-335
dc.description.codenJSBIE
dc.identifier.isiut000332815400011
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