dc.contributor.author | Zheng, Kai | |
dc.contributor.author | Laurence, Jennifer S. | |
dc.contributor.author | Kuczera, Krzysztof | |
dc.contributor.author | Verkhivker, Gennady M. | |
dc.contributor.author | Middaugh, C. Russell | |
dc.contributor.author | Siahaan, Teruna J. | |
dc.date.accessioned | 2017-05-31T21:25:20Z | |
dc.date.available | 2017-05-31T21:25:20Z | |
dc.date.issued | 2009-06 | |
dc.identifier.citation | 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 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24326 | |
dc.description.abstract | The 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.publisher | Wiley | en_US |
dc.subject | E-cadherin | en_US |
dc.subject | EC5 domain | en_US |
dc.subject | Conformation | en_US |
dc.subject | Spectroscopy | en_US |
dc.subject | Adherens junction | en_US |
dc.subject | Cell-cell adhesion | en_US |
dc.subject | Peptide binding | en_US |
dc.title | Characterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptides | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Zheng, Kai | |
kusw.kuauthor | Laurence, Jennifer S. | |
kusw.kuauthor | Krzysztof, Kuczera | |
kusw.kuauthor | Verkhivker, Gennady | |
kusw.kuauthor | Middaugh, C. Russell | |
kusw.kuauthor | Siahaan, Teruna J. | |
dc.identifier.doi | 10.1111/j.1747-0285.2009.00818.x | en_US |
dcterms.description | This 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.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3328966 | en_US |
dc.rights.accessrights | openAccess | |