 |
PDBsum entry 4zte
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
4zte
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of human e-Cadherin-Ec1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction.
|
|
|
Authors
|
|
V.Nardone,
A.P.Lucarelli,
A.Dalle vedove,
R.Fanelli,
A.Tomassetti,
L.Belvisi,
M.Civera,
E.Parisini.
|
|
|
Ref.
|
|
J Med Chem, 2016,
59,
5089-5094.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
