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dc.contributor.authorZheng, Kai
dc.contributor.authorLaurence, Jennifer S.
dc.contributor.authorKuczera, Krzysztof
dc.contributor.authorVerkhivker, Gennady M.
dc.contributor.authorMiddaugh, C. Russell
dc.contributor.authorSiahaan, Teruna J.
dc.date.accessioned2017-05-31T21:25:20Z
dc.date.available2017-05-31T21:25:20Z
dc.date.issued2009-06
dc.identifier.citationZheng, K., Laurence, J. S., Kuczera, K., Verkhivker, G., Russell Middaugh, C. and Siahaan, T. J. (2009), Characterization of Multiple Stable Conformers of the EC5 Domain of E-cadherin and the Interaction of EC5 with E-cadherin Peptides. Chemical Biology & Drug Design, 73: 584–598. doi:10.1111/j.1747-0285.2009.00818.xen_US
dc.identifier.urihttp://hdl.handle.net/1808/24326
dc.description.abstractThe objectives of this work were to express the EC5 domain of E-cadherin and determine its structural characteristics as well as to evaluate the binding properties of HAV and BLG4 peptides to EC5 using spectroscopic methods. Homophilic interactions of E-cadherins are responsible for cell-cell adhesion in the adherens junctions of the biological barriers (i.e., intestinal mucosa and blood-brain barriers). The EC5 domain of E-cadherin has an important role in T-cell adhesion to intestinal mucosa via αEβ7 integrin-E-cadherin interactions. In this study, the expressed EC5 has a high thermal stability (Tm = 64.3 °C); it also has two stable conformations at room temperature, which convert to one conformation at approximately 54.5 °C. NMR and FTIR showed that HAV and BLG4 peptides bind to EC5. HSQC-NMR showed that either Asn or Gln of EC5 was involved in the interactions with HAV and BLG4 peptides. EC5 underwent a conformational change upon interaction with the HAV and BLG4 peptides. Finally, the binding properties of both peptides were modeled by docking experiments, and the results suggest that Asn-46 and Asn-75 of EC5 could be involved during the interaction with the peptides and that the Ser and Trp residues of the HAV and BLG4 peptides, respectively, were important for binding to EC5.en_US
dc.publisherWileyen_US
dc.subjectE-cadherinen_US
dc.subjectEC5 domainen_US
dc.subjectConformationen_US
dc.subjectSpectroscopyen_US
dc.subjectAdherens junctionen_US
dc.subjectCell-cell adhesionen_US
dc.subjectPeptide bindingen_US
dc.titleCharacterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptidesen_US
dc.typeArticleen_US
kusw.kuauthorZheng, Kai
kusw.kuauthorLaurence, Jennifer S.
kusw.kuauthorKrzysztof, Kuczera
kusw.kuauthorVerkhivker, Gennady
kusw.kuauthorMiddaugh, C. Russell
kusw.kuauthorSiahaan, Teruna J.
dc.identifier.doi10.1111/j.1747-0285.2009.00818.xen_US
dcterms.descriptionThis is the peer reviewed version of the following article: Zheng, K., Laurence, J. S., Kuczera, K., Verkhivker, G., Russell Middaugh, C. and Siahaan, T. J. (2009), Characterization of Multiple Stable Conformers of the EC5 Domain of E-cadherin and the Interaction of EC5 with E-cadherin Peptides. Chemical Biology & Drug Design, 73: 584–598. doi:10.1111/j.1747-0285.2009.00818.x, which has been published in final form at http://doi.org/10.1111/j.1747-0285.2009.00818.x. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC3328966en_US
dc.rights.accessrightsopenAccess


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