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Teneurin 2 Partial Extracellular Domain
Structural highlights
FunctionTEN2_CHICK Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.[1] [2] [3] Ten-2 intracellular domain: Induces gene transcription inhibition. Publication Abstract from PubMedTeneurins 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. Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.,Jackson VA, Meijer DH, Carrasquero M, van Bezouwen LS, Lowe ED, Kleanthous C, Janssen BJC, Seiradake E Nat Commun. 2018 Mar 14;9(1):1079. doi: 10.1038/s41467-018-03460-0. PMID:29540701[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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