9bfu

Cryo-EM structure of Sevenless extracellular domain (composite map of the dimer, pH 4.6)

spinqualitylabelsall models 9bfu, resolution 4.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bfu is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.07Å Ligands: FUC, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 7LESS_DROME Receptor for an extracellular signal required to instruct a cell to differentiate into an R7 photoreceptor. The ligand for sev is the boss (bride of sevenless) protein on the surface of the neighboring R8 cell. Publication Abstract from PubMed Sevenless (Sev) is a Drosophila receptor tyrosine kinase (RTK) required for the specification of the R7 photoreceptor. It is cleaved into alpha and beta subunits and binds the ectodomain of the G-protein-coupled receptor bride of sevenless (Boss). Previous work showed that the Boss ectodomain could bind but not activate Sev; rather, the whole seven-pass transmembrane Boss was required. Here, we show that Sev does not need to be cleaved to function and that a single-pass transmembrane form of Boss activates Sev. We use cryo-electron microscopy and biophysical methods to determine the structural basis of ligand binding and pH-dependent dimerization of Sev, and we discuss the implications in the process of Sev activation. The Sev human homolog, receptor oncogene from sarcoma 1 (ROS1), is associated with oncogenic transformations, and we discuss their structural similarities. , PMID:39510067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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