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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.

Original publication

DOI

10.1038/s41467-018-03460-0

Type

Journal article

Journal

Nat Commun

Publication Date

14/03/2018

Volume

9

Keywords

Alternative Splicing, Cell Communication, Cryoelectron Microscopy, Crystallography, X-Ray, Membrane Glycoproteins, Platelet Glycoprotein GPIb-IX Complex, Protein Structure, Secondary, Tenascin