Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction
Teneurins are cell-cell adhesion receptors that evolved through horizontal gene transfer in which a bacterial YD-repeat protein fused to a eukaryotic receptor. Here the authors present crystallographic and cryo-EM structures of two Teneurins, revealing an ancient YD-repeat protein super-fold.
Guardado en:
Autores principales: | Verity A. Jackson, Dimphna H. Meijer, Maria Carrasquero, Laura S. van Bezouwen, Edward D. Lowe, Colin Kleanthous, Bert J. C. Janssen, Elena Seiradake |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/6e704646bfad422d89f023858d91ce18 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Super-complexes of adhesion GPCRs and neural guidance receptors
por: Verity A. Jackson, et al.
Publicado: (2016) -
Teneurins, TCAP, and latrophilins: roles in the etiology of mood disorders
por: Woelfle Rebecca, et al.
Publicado: (2016) -
Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism
por: Jingxian Li, et al.
Publicado: (2020) -
Exploring fold space preferences of new-born and ancient protein superfamilies.
por: Hannah Edwards, et al.
Publicado: (2013) -
The Ancient Link between G-Protein-Coupled Receptors and C-Terminal Phospholipid Kinase Domains
por: D. Johan van den Hoogen, et al.
Publicado: (2018)