4ZT1

Crystal structure of human E-Cadherin (residues 3-213) in x-dimer conformation

Summary for 4ZT1

• Entry DOI: 10.2210/pdb4zt1/pdb
• Descriptor: Cadherin-1, CALCIUM ION (3 entities in total)
• Functional Keywords: adhesion, cadherin, calcium-binding protein, x-dimer., cell adhesion
• Biological source: Homo sapiens (Human)
• Cellular location: Cell junction: P12830
• Total number of polymer chains: 2
• Total formula weight: 45939.32

Authors

Nardone, V.,Lucarelli, A.P.,Dalle Vedove, A.,Parisini, E. (deposition date: 2015-05-14, release date: 2016-06-01, Last modification date: 2024-01-10)

Primary citation

Nardone, V.,Lucarelli, A.P.,Dalle Vedove, A.,Fanelli, R.,Tomassetti, A.,Belvisi, L.,Civera, M.,Parisini, E.
Crystal Structure of Human E-Cadherin-EC1EC2 in Complex with a Peptidomimetic Competitive Inhibitor of Cadherin Homophilic Interaction.
J.Med.Chem., 59:5089-5094, 2016

PubMed 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.

PubMed: 27120112
DOI: 10.1021/acs.jmedchem.5b01487

Experimental method

X-RAY DIFFRACTION (1.92 Å)