9BFU
Cryo-EM structure of Sevenless extracellular domain (composite map of the dimer, pH 4.6)
Summary for 9BFU
| Entry DOI | 10.2210/pdb9bfu/pdb |
| Related | 9BFP 9BFQ 9BFR 9BFS |
| EMDB information | 44507 |
| Descriptor | Protein sevenless, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | sevenless, receptor tyrosine kinase, rtk, drosophila, eye development, vision, photoreceptor, ros1, signaling protein |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 456999.89 |
| Authors | Cerutti, G.,Shapiro, L. (deposition date: 2024-04-18, release date: 2025-01-29, Last modification date: 2025-06-04) |
| Primary citation | Cerutti, G.,Arias, R.,Bahna, F.,Mannepalli, S.,Katsamba, P.S.,Ahlsen, G.,Kloss, B.,Bruni, R.,Tomlinson, A.,Shapiro, L. Structures and pH-dependent dimerization of the sevenless receptor tyrosine kinase. Mol.Cell, 84:4677-4690.e6, 2024 Cited by PubMed Abstract: Sevenless (Sev) is a Drosophila receptor tyrosine kinase (RTK) required for the specification of the R7 photoreceptor. It is cleaved into α and β 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. PubMed: 39510067DOI: 10.1016/j.molcel.2024.10.017 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.07 Å) |
Structure validation
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