6FAY
Teneurin3 monomer
Summary for 6FAY
| Entry DOI | 10.2210/pdb6fay/pdb |
| EMDB information | 4219 |
| Descriptor | Odz3 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | neuronal cell adhesion, bacterial toxin-like, cell adhesion |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 212535.77 |
| Authors | Janssen, B.J.C.,Meijer, D.H.M.,van Bezouwen, L.S. (deposition date: 2017-12-18, release date: 2018-03-28, Last modification date: 2024-10-23) |
| Primary citation | Jackson, V.A.,Meijer, D.H.,Carrasquero, M.,van Bezouwen, L.S.,Lowe, E.D.,Kleanthous, C.,Janssen, B.J.C.,Seiradake, E. Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction. Nat Commun, 9:1079-1079, 2018 Cited by PubMed Abstract: Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins. PubMed: 29540701DOI: 10.1038/s41467-018-03460-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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