6PNP
Crystal structure of the splice insert-free neurexin-1 LNS2 domain in complex with neurexophilin-1
Summary for 6PNP
| Entry DOI | 10.2210/pdb6pnp/pdb |
| Descriptor | Neurexin-1, Neurexophilin-1 (3 entities in total) |
| Functional Keywords | synapse, complex, splice-variant, cell adhesion |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 40215.18 |
| Authors | Wilson, S.C.,White, K.I.,Zhou, Q.,Brunger, A.T. (deposition date: 2019-07-02, release date: 2019-10-09, Last modification date: 2024-10-23) |
| Primary citation | Wilson, S.C.,White, K.I.,Zhou, Q.,Pfuetzner, R.A.,Choi, U.B.,Sudhof, T.C.,Brunger, A.T. Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing. Embo J., 38:e101603-e101603, 2019 Cited by PubMed Abstract: Neurexins are presynaptic, cell-adhesion molecules that specify the functional properties of synapses via interactions with trans-synaptic ligands. Neurexins are extensively alternatively spliced at six canonical sites that regulate multifarious ligand interactions, but the structural mechanisms underlying alternative splicing-dependent neurexin regulation are largely unknown. Here, we determined high-resolution structures of the complex of neurexophilin-1 and the second laminin/neurexin/sex-hormone-binding globulin domain (LNS2) of neurexin-1 and examined how alternative splicing at splice site #2 (SS2) regulates the complex. Our data reveal a unique, extensive, neurexophilin-neurexin binding interface that extends the jelly-roll β-sandwich of LNS2 of neurexin-1 into neurexophilin-1. The SS2A insert of LNS2 augments this interface, increasing the binding affinity of LNS2 for neurexophilin-1. Taken together, our data reveal an unexpected architecture of neurexophilin-neurexin complexes that accounts for the modulation of binding by alternative splicing, which in turn regulates the competition of neurexophilin for neurexin binding with other ligands. PubMed: 31566781DOI: 10.15252/embj.2019101603 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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