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    Characterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptides

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    Zheng_2009.pdf (3.523Mb)
    Issue Date
    2009-06
    Author
    Zheng, Kai
    Laurence, Jennifer S.
    Kuczera, Krzysztof
    Verkhivker, Gennady M.
    Middaugh, C. Russell
    Siahaan, Teruna J.
    Publisher
    Wiley
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
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    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.
    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.
    URI
    http://hdl.handle.net/1808/24326
    DOI
    https://doi.org/10.1111/j.1747-0285.2009.00818.x
    Collections
    • Pharmaceutical Chemistry Scholarly Works [336]
    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

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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