Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions

ABSTRACT: Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic and heterophilic interactions, and is required for synaptic partner matching in the visual and hippocampal systems in vertebrates. It remains unclear how individual teneurins form macromolecular cis- and trans-synaptic protein complexes. Here, we present a 2.7 Å cryo-EM structure of the dimeric ectodomain of human Teneurin4. The structure reveals a compact conformation of the dimer, stabilized by interactions mediated by the C-rich, YD-shell, and ABD domains. A 1.5 Å crystal structure of the C-rich domain shows three conserved calcium binding sites, and thermal unfolding assays and SAXS-based rig

SUBMITTER: Dr. Bert Janssen 

PROVIDER: S-SCDT-EMBOJ-2020-107505 | biostudies-other |

REPOSITORIES: biostudies-other