9NSA
Crystal Structure of Side-VII IG1 Domain
Summary for 9NSA
| Entry DOI | 10.2210/pdb9nsa/pdb |
| Related | 9NP7 9NQ2 9NS8 |
| Descriptor | Sidestep VII (2 entities in total) |
| Functional Keywords | immunoglobulin superfamily, protein binding, neuronal, cell surface receptor, cell adhesion |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 14582.28 |
| Authors | Olechwier, A.M.,Ozkan, E. (deposition date: 2025-03-16, release date: 2026-06-10, Last modification date: 2026-07-01) |
| Primary citation | Priest, J.M.,Zhang, R.,Olechwier, A.M.,Caspi-Lebovic, A.B.,Ashley, J.,Aher, V.,Carrillo, R.A.,Ozkan, E. Structural insights into wiring specificity in the neuromuscular system through the Beat-Side complex. Biorxiv, 2025 Cited by PubMed Abstract: Nervous system assembly is guided by the actions of cell surface receptors. In , members of the Beaten Path (Beat) and Sidestep (Side) protein families have been described as axon guidance receptor-cue pairs, in addition to roles in specifying synaptic connectivity in the optic lobe. To understand the molecular basis and specificity of Beat-Side interactions, we report here the first Beat-Side structure, Beat-Vc bound to Side-VI. The structure showed a binding topology similar to other neuronal immunoglobulin superfamily receptors, especially Nectins, SynCAMs, Dprs and DIPs, despite lack of established evolutionary relationships. Using a structure-based rational approach, we engineered and validated point mutations to break the binding between Beats and Sides. Using these mutant variants, we demonstrated in developing larvae that the interaction between Beat-Ia and Side is required for establishing proper connectivity of motor neurons with muscles. PubMed: 40661433DOI: 10.1101/2025.06.05.656487 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
Download full validation report
