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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural insights into the contactin 1 - neurofascin 155 adhesion complex Lucas M. P. Chataigner , Christos Gogou , Maurits A. Den Boer , Cátia P. Frias , Dominique M. E. Thies-Weesie , Joke C. M. Granneman , Albert J. R. Heck , Dimphna H. Meijer , Bert J. C. Janssen Nature Communications 13 DOI: 10.1038/s41467-022-34302-9 Diamond Proposal Number(s): [19800] Open Access Show Abstract ▼ Abstract: Cell-surface expressed contactin 1 and neurofascin 155 control wiring of the nervous system and interact across cells to form and maintain paranodal myelin-axon junctions. The molecular mechanism of contactin 1 – neurofascin 155 adhesion complex formation is unresolved. Crystallographic structures of complexed and individual contactin 1 and neurofascin 155 binding regions presented here, provide a rich picture of how competing and complementary interfaces, post-translational glycosylation, splice differences and structural plasticity enable formation of diverse adhesion sites. Structural, biophysical, and cell-clustering analysis reveal how conserved Ig1-2 interfaces form competing heterophilic contactin 1 – neurofascin 155 and homophilic neurofascin 155 complexes whereas contactin 1 forms low-affinity clusters through interfaces on Ig3-6. The structures explain how the heterophilic Ig1-Ig4 horseshoe’s in the contactin 1 – neurofascin 155 complex define the 7.4 nm paranodal spacing and how the remaining six domains enable bridging of distinct intercellular distances.	Nov 2022
B21-High Throughput SAXS	Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions Dimphna H Meijer , Cátia P Frias , J. Wouter Beugelink , Yanthi N. Deurloo , Bert J. C. Janssen The Embo Journal 66 DOI: 10.15252/embj.2020107505 Diamond Proposal Number(s): [19800] Open Access Show Abstract ▼ 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 rigid-body modeling demonstrate that the compactness and stability of Teneurin4 dimers are calcium-dependent. Teneurin4 dimers form a more extended conformation in conditions that lack calcium. Cellular assays reveal that the compact cis-dimer is compatible with homomeric trans-interactions. Together, these findings support a role for teneurins as a scaffold for macromolecular complex assembly and the establishment of cis- and trans-synaptic interactions to construct functional neuronal circuits.	Jan 2022

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