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.
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]
Crystal structure of human E-cadherin-EC1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction
L. Belvisi;M. CiveraPenultimo
;
2016
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.File | Dimensione | Formato | |
---|---|---|---|
JMedChem2016_PostPrint_accettato.pdf
accesso aperto
Tipologia:
Post-print, accepted manuscript ecc. (versione accettata dall'editore)
Dimensione
558.27 kB
Formato
Adobe PDF
|
558.27 kB | Adobe PDF | Visualizza/Apri |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.