6ska

Teneurin 2 in complex with Latrophilin 1 Lec-Olf domains

spinqualitylabelsall models 6ska, resolution 3.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ska is a 2 chain structure with sequence from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.86Å Ligands: BMA, CA, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TEN2_CHICK Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer. Ten-2 intracellular domain: Induces gene transcription inhibition. Publication Abstract from PubMed Teneurins are ancient metazoan cell adhesion receptors that control brain development and neuronal wiring in higher animals. The extracellular C terminus binds the adhesion GPCR Latrophilin, forming a trans-cellular complex with synaptogenic functions. However, Teneurins, Latrophilins, and FLRT proteins are also expressed during murine cortical cell migration at earlier developmental stages. Here, we present crystal structures of Teneurin-Latrophilin complexes that reveal how the lectin and olfactomedin domains of Latrophilin bind across a spiraling beta-barrel domain of Teneurin, the YD shell. We couple structure-based protein engineering to biophysical analysis, cell migration assays, and in utero electroporation experiments to probe the importance of the interaction in cortical neuron migration. We show that binding of Latrophilins to Teneurins and FLRTs directs the migration of neurons using a contact repulsion-dependent mechanism. The effect is observed with cell bodies and small neurites rather than their processes. The results exemplify how a structure-encoded synaptogenic protein complex is also used for repulsive cell guidance. Structural Basis of Teneurin-Latrophilin Interaction in Repulsive Guidance of Migrating Neurons.,Del Toro D, Carrasquero-Ordaz MA, Chu A, Ruff T, Shahin M, Jackson VA, Chavent M, Berbeira-Santana M, Seyit-Bremer G, Brignani S, Kaufmann R, Lowe E, Klein R, Seiradake E Cell. 2020 Jan 23;180(2):323-339.e19. doi: 10.1016/j.cell.2019.12.014. Epub 2020 , Jan 9. PMID:31928845 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Latrophilin

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