Crystal structure of human E-cadherin-EC1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction
Articolo
Data di Pubblicazione:
2016
Citazione:
Crystal structure of human E-cadherin-EC1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction / V. Nardone, A.P. Lucarelli, A. Dalle Vedove, R. Fanelli, A. Tomassetti, L. Belvisi, M. Civera, E. Parisini. - In: JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0022-2623. - 59:10(2016 Apr 27), pp. 5089-5094. [10.1021/acs.jmedchem.5b01487]
Abstract:
Cadherins are transmembrane cell adhesion proteins whose aberrant expression often correlates with cancer development and proliferation. We report the crystal structure of an E-cadherin extracellular fragment in complex with a peptidomimetic compound that was previously shown to partially inhibit cadherin homophilic adhesion. The structure reveals an unexpected binding mode and allows the identification of a druggable cadherin interface, thus paving the way to a future structure-guided design of cell adhesion inhibitors against cadherin-expressing solid tumors.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
cell-adhesion; classic cadherins; dimerization; mechanism; activation; binding; identification; specificity; antagonists; arthritis
Elenco autori:
V. Nardone, A.P. Lucarelli, A. Dalle Vedove, R. Fanelli, A. Tomassetti, L. Belvisi, M. Civera, E. Parisini
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