9NSF

Crystal Structure of the Complex of Side-VI IG1 Domain and Beat-Vc IG1+2 Domains

Summary for 9NSF

• Entry DOI: 10.2210/pdb9nsf/pdb
• Related: 9NP7 9NQ2 9NS8 9NSA
• Descriptor: Beaten path Vc, Sidestep VI, isoform B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: immunoglobulin superfamily, glycoprotein, complex, cell surface receptor, cell adhesion
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 4
• Total formula weight: 88679.90

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

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: 40661433
DOI: 10.1101/2025.06.05.656487

Experimental method

X-RAY DIFFRACTION (3.93 Å)