Autor: |
Jackson, Verity A, Meijer, Dimphna H, Carrasquero, Maria, van Bezouwen, Laura S, Lowe, Edward D, Kleanthous, Colin, Janssen, Bert J C, Seiradake, Elena, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Sub Cryo - EM, Cryo-EM |
Jazyk: |
angličtina |
Rok vydání: |
2018 |
Předmět: |
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Zdroj: |
Nature Communications, 9(1). Nature Publishing Group |
ISSN: |
2041-1723 |
Popis: |
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. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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