4ZMP
Crystal structure of human P-cadherin (ss-dimer Q101L)
Summary for 4ZMP
| Entry DOI | 10.2210/pdb4zmp/pdb |
| Related | 4zml 4zmn 4zmo 4zmq 4zmt 4zmv 4zmw 4zmx 4zmy 4zmz |
| Descriptor | Cadherin-3, CALCIUM ION (3 entities in total) |
| Functional Keywords | dimerization, conformational change, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23396.08 |
| Authors | Caaveiro, J.M.M.,Kudo, S.,Tsumoto, K. (deposition date: 2015-05-04, release date: 2016-09-07, Last modification date: 2023-11-08) |
| Primary citation | Kudo, S.,Caaveiro, J.M.,Tsumoto, K. Adhesive Dimerization of Human P-Cadherin Catalyzed by a Chaperone-like Mechanism Structure, 24:1523-1536, 2016 Cited by PubMed Abstract: Orderly assembly of classical cadherins governs cell adhesion and tissue maintenance. A key event is the strand-swap dimerization of the extracellular ectodomains of two cadherin molecules from apposing cells. Here we have determined crystal structures of P-cadherin in six different conformational states to elaborate a motion picture of its adhesive dimerization at the atomic level. The snapshots revealed that cell-adhesive dimerization is facilitated by several intermediate states collectively termed X-dimer in analogy to other classical cadherins. Based on previous studies and on the combined structural, kinetic, thermodynamic, biochemical, and cellular data reported herein, we propose that the adhesive dimerization of human P-cadherin is achieved by a stepwise mechanism analogous to that of assembly chaperones. This mechanism, applicable to type I classical cadherins, confers high specificity and fast association rates. We expect these findings to guide innovative therapeutic approaches targeting P-cadherin in cancer. PubMed: 27545624DOI: 10.1016/j.str.2016.07.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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