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-Structure paper
タイトル | Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 1079, Year 2018 |
掲載日 | 2018年3月14日 |
著者 | Verity A Jackson / Dimphna H Meijer / Maria Carrasquero / Laura S van Bezouwen / Edward D Lowe / Colin Kleanthous / Bert J C Janssen / Elena Seiradake / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:29540701 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.38 - 3.8 Å |
構造データ | PDB-6fb3: |
化合物 | ChemComp-NAG: ChemComp-HOH: |
由来 |
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キーワード | CELL ADHESION / Neuronal cell adhesion / bacterial toxin-like / TTR / fibronectin / FN-plug / NHL / YD-repeat / antibiotic-binding / colicin / nuclease / cell surface receptor / latrophilin / glycoprotein |