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 Cited by 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: 27120112DOI: 10.1021/acs.jmedchem.5b01487 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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